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Genome polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Protein P3; 6 kDa protein 1 (6K1); Cytoplasmic inclusion protein (CI) (EC 3.6.4.-); 6 kDa protein 2 (6K2); Viral genome-linked protein (VPg); Nuclear inclusion protein A (NI-a) (NIa) (EC 3.4.22.44) (49 kDa proteinase) (49 kDa-Pro) (NIa-pro); Nuclear inclusion protein B (NI-b) (NIb) (EC 2.7.7.48) (RNA-directed RNA polymerase); Capsid protein (CP) (Coat protein)]

 POLG_TEV                Reviewed;        3054 AA.
P04517; Q88500; Q88501; Q88502; Q88504; Q88505; Q88506; Q89773;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P1 proteinase;
EC=3.4.-.-;
AltName: Full=N-terminal protein;
Contains:
RecName: Full=Helper component proteinase;
Short=HC-pro;
EC=3.4.22.45;
Contains:
RecName: Full=Protein P3;
Contains:
RecName: Full=6 kDa protein 1;
Short=6K1;
Contains:
RecName: Full=Cytoplasmic inclusion protein;
Short=CI;
EC=3.6.4.-;
Contains:
RecName: Full=6 kDa protein 2;
Short=6K2;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
Contains:
RecName: Full=Nuclear inclusion protein A;
Short=NI-a;
Short=NIa;
EC=3.4.22.44;
AltName: Full=49 kDa proteinase;
Short=49 kDa-Pro;
AltName: Full=NIa-pro;
Contains:
RecName: Full=Nuclear inclusion protein B;
Short=NI-b;
Short=NIb;
EC=2.7.7.48;
AltName: Full=RNA-directed RNA polymerase;
Contains:
RecName: Full=Capsid protein;
Short=CP;
AltName: Full=Coat protein;
Tobacco etch virus (TEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Potyviridae; Potyvirus.
NCBI_TaxID=12227;
NCBI_TaxID=4072; Capsicum annuum (Bell pepper).
NCBI_TaxID=53851; Cassia.
NCBI_TaxID=4076; Datura stramonium (Jimsonweed) (Common thornapple).
NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
NCBI_TaxID=24663; Physalis.
NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Allison R., Johnston R.E., Dougherty W.G.;
"The nucleotide sequence of the coding region of tobacco etch virus
genomic RNA: evidence for the synthesis of a single polyprotein.";
Virology 154:9-20(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2344-3054.
PubMed=16593574; DOI=10.1073/pnas.82.12.3969;
Allison R.F., Sorenson J.C., Kelly M.E., Armstrong F.B.,
Dougherty W.G.;
"Sequence determination of the capsid protein gene and flanking
regions of tobacco etch virus: evidence for synthesis and processing
of a polyprotein in potyvirus genome expression.";
Proc. Natl. Acad. Sci. U.S.A. 82:3969-3972(1985).
[3]
IDENTIFICATION OF PROTEASES.
PubMed=2656254;
Carrigton J.C., Cary S.M., Parks T.D., Dougherty W.G.;
"A second proteinase encoded by a plant potyvirus genome.";
EMBO J. 8:365-370(1989).
[4]
ACTIVE SITES OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF
SER-610; HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675;
ASP-689; CYS-694; SER-698; ASP-715; HIS-716; HIS-722; ASP-725;
SER-726; HIS-735; SER-743 AND SER-755.
PubMed=2688301; DOI=10.1016/0042-6822(89)90582-5;
Oh C.-S., Carrington J.C.;
"Identification of essential residues in potyvirus proteinase HC-Pro
by site-directed mutagenesis.";
Virology 173:692-699(1989).
[5]
ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A.
PubMed=2475971; DOI=10.1016/0042-6822(89)90132-3;
Dougherty W.G., Parks T.D., Cary S.M., Bazan J.F., Fletterick R.J.;
"Characterization of the catalytic residues of the tobacco etch virus
49-kDa proteinase.";
Virology 172:302-310(1989).
[6]
ACTIVE SITES OF P1 PROTEINASE, AND MUTAGENESIS OF HIS-214 AND SER-256.
PubMed=1962435; DOI=10.1016/0042-6822(91)90522-D;
Verchot J., Koonin E.V., Carrington J.C.;
"The 35-kDa protein from the N-terminus of the potyviral polyprotein
functions as a third virus-encoded proteinase.";
Virology 185:527-535(1991).
[7]
FUNCTION OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF PHE-314
AND LYS-358.
PubMed=9880030;
Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C.,
Baker J., Pirone T.P.;
"Mutations in the potyvirus helper component protein: effects on
interactions with virions and aphid stylets.";
J. Gen. Virol. 79:3119-3122(1998).
[8]
FUNCTION OF HELPER COMPONENT PROTEINASE.
PubMed=11414807; DOI=10.1006/viro.2001.0901;
Kasschau K.D., Carrington J.C.;
"Long-distance movement and replication maintenance functions
correlate with silencing suppression activity of potyviral HC-Pro.";
Virology 285:71-81(2001).
[9]
REVIEW.
PubMed=11226583; DOI=10.1016/S0168-1702(01)00220-9;
Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
"Potyvirus proteins: a wealth of functions.";
Virus Res. 74:157-175(2001).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2038-2794, SUBUNIT, AND
DISULFIDE BOND.
PubMed=12377789; DOI=10.1074/jbc.M207224200;
Phan J., Zdanov A., Evdokimov A.G., Tropea J.E., Peters H.K. III,
Kapust R.B., Li M., Wlodawer A., Waugh D.S.;
"Structural basis for the substrate specificity of tobacco etch virus
protease.";
J. Biol. Chem. 277:50564-50572(2002).
[11]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2038-2279, SUBUNIT, DISULFIDE
BOND, AND ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A.
PubMed=15919091; DOI=10.1016/j.jmb.2005.04.013;
Nunn C.M., Jeeves M., Cliff M.J., Urquhart G.T., George R.R.,
Chao L.H., Tscuchia Y., Djordjevic S.;
"Crystal structure of tobacco etch virus protease shows the protein C
terminus bound within the active site.";
J. Mol. Biol. 350:145-155(2005).
-!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to-
cell and systemis movement, encapsidation of the viral RNA and in
the regulation of viral RNA amplification.
-!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA
polymerase that plays an essential role in the virus replication.
-!- FUNCTION: Helper component proteinase: required for aphid
transmission and also has proteolytic activity. Only cleaves a
Gly-Gly dipeptide at its own C-terminus. Interacts with virions
and aphid stylets. Acts as a suppressor of RNA-mediated gene
silencing, also known as post-transcriptional gene silencing
(PTGS), a mechanism of plant viral defense that limits the
accumulation of viral RNAs. May have RNA-binding activity.
-!- FUNCTION: Cytoplasmic inclusion protein: has helicase activity. It
may be involved in replication.
-!- FUNCTION: Both 6K peptides are indispensable for virus
replication. {ECO:0000250, ECO:0000269|PubMed:11414807,
ECO:0000269|PubMed:9880030}.
-!- FUNCTION: Nuclear inclusion protein A: has RNA-binding and
proteolytic activities.
-!- CATALYTIC ACTIVITY: Hydrolyzes glutaminyl bonds, and activity is
further restricted by preferences for the amino acids in P6 - P1'
that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-
Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The
natural substrate is the viral polyprotein, but other proteins and
oligopeptides containing the appropriate consensus sequence are
also cleaved.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C-
terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
processing of the potyviral polyprotein.
-!- SUBUNIT: Nuclear inclusion protein A protease is a dimer;
disulfide-linked. {ECO:0000269|PubMed:12377789,
ECO:0000269|PubMed:15919091}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Genome polyprotein;
IsoId=P04517-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=P3N-PIPO polyprotein;
IsoId=P0CK09-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting in P3 ORF.;
-!- DOMAIN: The N-terminus of helper component proteinase is involved
in interaction with stylets. The central part is involved in
interaction with virions and the C-terminus is involved in cell-to
cell movement of the virus.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
attached to the 5'-end of the genomic RNA. This uridylylated form
acts as a nucleotide-peptide primer for the polymerase (By
similarity). {ECO:0000250}.
-!- PTM: Potyviral RNA is expressed as two polyproteins which undergo
post-translational proteolytic processing. Genome polyprotein is
processed by NIa-pro, P1 and HC-pro proteinases resulting in the
production of at least ten individual proteins. P3N-PIPO
polyprotein is cleaved by P1 and HC-pro proteinases resulting in
the production of three individual proteins. The P1 proteinase and
the HC-pro cleave only their respective C-termini
autocatalytically. 6K1 is essential for proper proteolytic
separation of P3 from CI (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
{ECO:0000305}.
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EMBL; M15239; AAA47910.1; -; Genomic_RNA.
EMBL; M11458; AAA47909.1; -; Genomic_RNA.
EMBL; M11216; AAA47908.1; ALT_SEQ; Genomic_RNA.
PIR; A04207; GNBVEV.
RefSeq; NP_062908.1; NC_001555.1. [P04517-1]
PDB; 1LVB; X-ray; 2.20 A; A/B=2038-2273, C/D=2785-2794.
PDB; 1LVM; X-ray; 1.80 A; A/B=2038-2258, C/D=2786-2794, E=2267-2273.
PDB; 1Q31; X-ray; 2.70 A; A/B=2038-2279.
PDBsum; 1LVB; -.
PDBsum; 1LVM; -.
PDBsum; 1Q31; -.
ProteinModelPortal; P04517; -.
SMR; P04517; -.
MEROPS; C04.004; -.
PRIDE; P04517; -.
GeneID; 1502321; -.
KEGG; vg:1502321; -.
OrthoDB; VOG0900003L; -.
EvolutionaryTrace; P04517; -.
PMAP-CutDB; P04517; -.
Proteomes; UP000007404; Genome.
Proteomes; UP000201712; Genome.
GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR001456; HC-pro.
InterPro; IPR031159; HC_PRO_CPD_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR002540; Pept_S30_P1_potyvir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001592; Poty_coat.
InterPro; IPR001730; Potyv_NIa-pro_dom.
InterPro; IPR013648; PP_Potyviridae.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00863; Peptidase_C4; 1.
Pfam; PF00851; Peptidase_C6; 1.
Pfam; PF01577; Peptidase_S30; 1.
Pfam; PF00767; Poty_coat; 1.
Pfam; PF08440; Poty_PP; 1.
Pfam; PF00680; RdRP_1; 1.
PRINTS; PR00966; NIAPOTYPTASE.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51744; HC_PRO_CPD; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Capsid protein; Complete proteome;
Covalent protein-RNA linkage; Disulfide bond; Helical capsid protein;
Helicase; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; Ribosomal frameshifting;
RNA-directed RNA polymerase; Suppressor of RNA silencing;
Thiol protease; Transferase; Viral RNA replication; Virion.
CHAIN 1 3054 Genome polyprotein.
/FTId=PRO_0000420026.
CHAIN 1 304 P1 proteinase. {ECO:0000255}.
/FTId=PRO_0000040450.
CHAIN 305 763 Helper component proteinase.
{ECO:0000255}.
/FTId=PRO_0000040451.
CHAIN 764 1110 Protein P3. {ECO:0000250}.
/FTId=PRO_0000040452.
CHAIN 1111 1163 6 kDa protein 1. {ECO:0000250}.
/FTId=PRO_0000040453.
CHAIN 1164 1796 Cytoplasmic inclusion protein.
/FTId=PRO_0000040454.
CHAIN 1797 1849 6 kDa protein 2.
/FTId=PRO_0000040455.
CHAIN 1850 2037 Viral genome-linked protein.
{ECO:0000250}.
/FTId=PRO_0000040456.
CHAIN 2038 2279 Nuclear inclusion protein A.
{ECO:0000250}.
/FTId=PRO_0000040457.
CHAIN 2280 2791 Nuclear inclusion protein B.
/FTId=PRO_0000040458.
CHAIN 2792 3054 Capsid protein.
/FTId=PRO_0000040459.
DOMAIN 641 763 Peptidase C6. {ECO:0000255|PROSITE-
ProRule:PRU01080}.
DOMAIN 1234 1386 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1401 1564 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 2038 2255 Peptidase C4. {ECO:0000255|PROSITE-
ProRule:PRU00766}.
DOMAIN 2521 2641 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1247 1254 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 358 361 Involved in interaction with stylet and
aphid transmission.
MOTIF 615 617 Involved in virions binding and aphid
transmission. {ECO:0000250}.
MOTIF 1336 1339 DECH box.
MOTIF 1889 1896 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 214 214 For P1 proteinase activity.
ACT_SITE 223 223 For P1 proteinase activity.
{ECO:0000255}.
ACT_SITE 256 256 For P1 proteinase activity.
ACT_SITE 649 649 For helper component proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01080}.
ACT_SITE 722 722 For helper component proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01080}.
ACT_SITE 2083 2083 For nuclear inclusion protein A activity.
ACT_SITE 2118 2118 For nuclear inclusion protein A activity.
ACT_SITE 2188 2188 For nuclear inclusion protein A activity.
SITE 304 305 Cleavage; by P1 proteinase.
{ECO:0000255}.
SITE 763 764 Cleavage; by autolysis.
{ECO:0000255|PROSITE-ProRule:PRU01080}.
SITE 1110 1111 Cleavage; by NIa-pro. {ECO:0000250}.
SITE 1163 1164 Cleavage; by NIa-pro. {ECO:0000250}.
SITE 1796 1797 Cleavage; by NIa-pro. {ECO:0000250}.
SITE 1849 1850 Cleavage; by NIa-pro. {ECO:0000250}.
SITE 2037 2038 Cleavage; by NIa-pro. {ECO:0000250}.
SITE 2279 2280 Cleavage; by NIa-pro. {ECO:0000250}.
SITE 2791 2792 Cleavage; by NIa-pro. {ECO:0000250}.
MOD_RES 1911 1911 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
DISULFID 2167 2167 Interchain. {ECO:0000269|PubMed:12377789,
ECO:0000269|PubMed:15919091}.
MUTAGEN 214 214 H->A: Complete loss of proteolytic
activity of P1 proteinase.
{ECO:0000269|PubMed:1962435}.
MUTAGEN 256 256 S->A: Complete loss of proteolytic
activity of P1 proteinase.
{ECO:0000269|PubMed:1962435}.
MUTAGEN 314 314 F->L: Complete loss of aphid
transmission.
{ECO:0000269|PubMed:9880030}.
MUTAGEN 358 358 K->E: Complete loss of interaction with
stylet and aphid transmission; no effect
on virion binding.
{ECO:0000269|PubMed:9880030}.
MUTAGEN 610 610 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 619 619 H->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 625 625 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 627 627 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 632 632 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 649 649 C->S: Complete loss of proteolytic
activity of HC-pro.
{ECO:0000269|PubMed:2688301}.
MUTAGEN 675 675 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 689 689 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 694 694 C->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 698 698 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 715 715 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 716 716 H->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 722 722 H->S: Complete loss of proteolytic
activity of HC-pro.
{ECO:0000269|PubMed:2688301}.
MUTAGEN 725 725 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 726 726 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 729 729 S->T: No effect on proteolytic activity
of HC-pro.
MUTAGEN 735 735 H->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 743 743 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 755 755 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
HELIX 2038 2040 {ECO:0000244|PDB:1LVM}.
HELIX 2049 2052 {ECO:0000244|PDB:1LVM}.
STRAND 2055 2062 {ECO:0000244|PDB:1LVM}.
STRAND 2065 2074 {ECO:0000244|PDB:1LVM}.
STRAND 2077 2080 {ECO:0000244|PDB:1LVM}.
HELIX 2082 2086 {ECO:0000244|PDB:1LVM}.
STRAND 2089 2096 {ECO:0000244|PDB:1LVM}.
STRAND 2099 2104 {ECO:0000244|PDB:1LVM}.
HELIX 2106 2108 {ECO:0000244|PDB:1LVM}.
STRAND 2109 2113 {ECO:0000244|PDB:1LVM}.
STRAND 2120 2123 {ECO:0000244|PDB:1LVM}.
STRAND 2145 2152 {ECO:0000244|PDB:1LVM}.
STRAND 2154 2157 {ECO:0000244|PDB:1LVM}.
STRAND 2159 2162 {ECO:0000244|PDB:1LVM}.
STRAND 2169 2171 {ECO:0000244|PDB:1LVM}.
TURN 2172 2175 {ECO:0000244|PDB:1LVM}.
STRAND 2176 2179 {ECO:0000244|PDB:1LVM}.
STRAND 2191 2194 {ECO:0000244|PDB:1LVM}.
TURN 2195 2197 {ECO:0000244|PDB:1LVM}.
STRAND 2200 2208 {ECO:0000244|PDB:1LVM}.
STRAND 2209 2211 {ECO:0000244|PDB:1Q31}.
STRAND 2213 2218 {ECO:0000244|PDB:1LVM}.
HELIX 2223 2228 {ECO:0000244|PDB:1LVM}.
HELIX 2230 2232 {ECO:0000244|PDB:1LVM}.
STRAND 2235 2238 {ECO:0000244|PDB:1LVM}.
STRAND 2243 2248 {ECO:0000244|PDB:1LVM}.
STRAND 2251 2256 {ECO:0000244|PDB:1LVM}.
STRAND 2276 2278 {ECO:0000244|PDB:1Q31}.
STRAND 2788 2790 {ECO:0000244|PDB:1LVM}.
SEQUENCE 3054 AA; 346164 MW; 0AF9A3626960B5CE CRC64;
MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH KPVIFGEDYI
TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN NKRNRRRKVA KTYVGRDSIV
EKIVVPHTER KVDTTAAVED ICNEATTQLV HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV
RKRHMQVEII SKKSVRARVK RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR
FKNERVDQSK LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS
MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT QALSPCGKIT
CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA EKLLTRFLQQ KSLVNTNLTA
CVSVKQLIGD RKQAPFTHVL AVSEILFKGN KLTGADLEEA STHMLEIARF LNNRTENMRI
GHLGSFRNKI SSKAHVNNAL MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK
YVIRKHIRGS RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV
TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY MNIFFALLVN
VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL YPDVLRAELP RILVDHDNKT
MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH SGLESEMKTY NVGGMNRDVV TQGAIEMLIK
SIYKPHLMKQ LLEEEPYIIV LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS
ALAQKLTLAD LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL
REGGYAVTSE KVHEMLEKNY VKALKDAWDE LTWLEKFSAI RHSRKLLKFG RKPLIMKNTV
DCGGHIDLSV KSLFKFHLEL LKGTISRAVN GGARKVRVAK NAMTKGVFLK IYSMLPDVYK
FITVSSVLSL LLTFLFQIDC MIRAHREAKV AAQLQKESEW DNIINRTFQY SKLENPIGYR
STAEERLQSE HPEAFEYYKF CIGKEDLVEQ AKQPEIAYFE KIIAFITLVL MAFDAERSDG
VFKILNKFKG ILSSTEREII YTQSLDDYVT TFDDNMTINL ELNMDELHKT SLPGVTFKQW
WNNQISRGNV KPHYRTEGHF MEFTRDTAAS VASEISHSPA RDFLVRGAVG SGKSTGLPYH
LSKRGRVLML EPTRPLTDNM HKQLRSEPFN CFPTLRMRGK STFGSSPITV MTSGFALHHF
ARNIAEVKTY DFVIIDECHV NDASAIAFRN LLFEHEFEGK VLKVSATPPG REVEFTTQFP
VKLKIEEALS FQEFVSLQGT GANADVISCG DNILVYVASY NDVDSLGKLL VQKGYKVSKI
DGRTMKSGGT EIITEGTSVK KHFIVATNII ENGVTIDIDV VVDFGTKVVP VLDVDNRAVQ
YNKTVVSYGE RIQKLGRVGR HKEGVALRIG QTNKTLVEIP EMVATEAAFL CFMYNLPVTT
QSVSTTLLEN ATLLQARTMA QFELSYFYTI NFVRFDGSMH PVIHDKLKRF KLHTCETFLN
KLAIPNKGLS SWLTSGEYKR LGYIAEDAGI RIPFVCKEIP DSLHEEIWHI VVAHKGDSGI
GRLTSVQAAK VVYTLQTDVH SIARTLACIN RRIADEQMKQ SHFEAATGRA FSFTNYSIQS
IFDTLKANYA TKHTKENIAV LQQAKDQLLE FSNLAKDQDV TGIIQDFNHL ETIYLQSDSE
VAKHLKLKSH WNKSQITRDI IIALSVLIGG GWMLATYFKD KFNEPVYFQG KKNQKHKLKM
REARGARGQY EVAAEPEALE HYFGSAYNNK GKRKGTTRGM GAKSRKFINM YGFDPTDFSY
IRFVDPLTGH TIDESTNAPI DLVQHEFGKV RTRMLIDDEI EPQSLSTHTT IHAYLVNSGT
KKVLKVDLTP HSSLRASEKS TAIMGFPERE NELRQTGMAV PVAYDQLPPK NEDLTFEGES
LFKGPRDYNP ISSTICHLTN ESDGHTTSLY GIGFGPFIIT NKHLFRRNNG TLLVQSLHGV
FKVKNTTTLQ QHLIDGRDMI IIRMPKDFPP FPQKLKFREP QREERICLVT TNFQTKSMSS
MVSDTSCTFP SSDGIFWKHW IQTKDGQCGS PLVSTRDGFI VGIHSASNFT NTNNYFTSVP
KNFMELLTNQ EAQQWVSGWR LNADSVLWGG HKVFMSKPEE PFQPVKEATQ LMNELVYSQG
EKRKWVVEAL SGNLRPVAEC PSQLVTKHVV KGKCPLFELY LQLNPEKEAY FKPMMGAYKP
SRLNREAFLK DILKYASEIE IGNVDCDLLE LAISMLVTKL KALGFPTVNY ITDPEEIFSA
LNMKAAMGAL YKGKKKEALS ELTLDEQEAM LKASCLRLYT GKLGIWNGSL KAELRPIEKV
ENNKTRTFTA APIDTLLAGK VCVDDFNNQF YDLNIKAPWT VGMTKFYQGW NELMEALPSG
WVYCDADGSQ FDSSLTPFLI NAVLKVRLAF MEEWDIGEQM LRNLYTEIVY TPILTPDGTI
IKKHKGNNSG QPSTVVDNTL MVIIAMLYTC EKCGINKEEI VYYVNGDDLL IAIHPDKAER
LSRFKESFGE LGLKYEFDCT TRDKTQLWFM SHRALERDGM YIPKLEEERI VSILEWDRSK
EPSHRLEAIC ASMIEAWGYD KLVEEIRNFY AWVLEQAPYS QLAEEGKAPY LAETALKFLY
TSQHGTNSEI EEYLKVLYDY DIPTTENLYF QSGTVDAGAD AGKKKDQKDD KVAEQASKDR
DVNAGTSGTF SVPRINAMAT KLQYPRMRGE VVVNLNHLLG YKPQQIDLSN ARATHEQFAA
WHQAVMTAYG VNEEQMKILL NGFMVWCIEN GTSPNLNGTW VMMDGEDQVS YPLKPMVENA
QPTLRQIMTH FSDLAEAYIE MRNRERPYMP RYGLQRNITD MSLSRYAFDF YELTSKTPVR
AREAHMQMKA AAVRNSGTRL FGLDGNVGTA EEDTERHTAH DVNRNMHTLL GVRQ


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