GenomeNet

Database: UniProt
Entry: P04517
LinkDB: P04517
Original site: P04517 
ID   POLG_TEV                Reviewed;        3054 AA.
AC   P04517; Q88500; Q88501; Q88502; Q88504; Q88505; Q88506; Q89773;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   18-SEP-2019, entry version 168.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=Protein P3;
DE   Contains:
DE     RecName: Full=6 kDa protein 1;
DE              Short=6K1;
DE   Contains:
DE     RecName: Full=Cytoplasmic inclusion protein;
DE              Short=CI;
DE              EC=3.6.4.-;
DE   Contains:
DE     RecName: Full=6 kDa protein 2;
DE              Short=6K2;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein A;
DE              Short=NI-a;
DE              Short=NIa;
DE              EC=3.4.22.44;
DE     AltName: Full=49 kDa proteinase;
DE              Short=49 kDa-Pro;
DE     AltName: Full=NIa-pro;
DE   Contains:
DE     RecName: Full=Nuclear inclusion protein B;
DE              Short=NI-b;
DE              Short=NIb;
DE              EC=2.7.7.48;
DE     AltName: Full=RNA-directed RNA polymerase;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
OS   Tobacco etch virus (TEV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=12227;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=53851; Cassia.
OH   NCBI_TaxID=4076; Datura stramonium (Jimsonweed) (Common thornapple).
OH   NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH   NCBI_TaxID=24663; Physalis.
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Allison R., Johnston R.E., Dougherty W.G.;
RT   "The nucleotide sequence of the coding region of tobacco etch virus
RT   genomic RNA: evidence for the synthesis of a single polyprotein.";
RL   Virology 154:9-20(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2344-3054.
RX   PubMed=16593574; DOI=10.1073/pnas.82.12.3969;
RA   Allison R.F., Sorenson J.C., Kelly M.E., Armstrong F.B.,
RA   Dougherty W.G.;
RT   "Sequence determination of the capsid protein gene and flanking
RT   regions of tobacco etch virus: evidence for synthesis and processing
RT   of a polyprotein in potyvirus genome expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3969-3972(1985).
RN   [3]
RP   IDENTIFICATION OF PROTEASES.
RX   PubMed=2656254; DOI=10.1002/j.1460-2075.1989.tb03386.x;
RA   Carrigton J.C., Cary S.M., Parks T.D., Dougherty W.G.;
RT   "A second proteinase encoded by a plant potyvirus genome.";
RL   EMBO J. 8:365-370(1989).
RN   [4]
RP   ACTIVE SITES OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF
RP   SER-610; HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675;
RP   ASP-689; CYS-694; SER-698; ASP-715; HIS-716; HIS-722; ASP-725;
RP   SER-726; HIS-735; SER-743 AND SER-755.
RX   PubMed=2688301; DOI=10.1016/0042-6822(89)90582-5;
RA   Oh C.-S., Carrington J.C.;
RT   "Identification of essential residues in potyvirus proteinase HC-Pro
RT   by site-directed mutagenesis.";
RL   Virology 173:692-699(1989).
RN   [5]
RP   ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A.
RX   PubMed=2475971; DOI=10.1016/0042-6822(89)90132-3;
RA   Dougherty W.G., Parks T.D., Cary S.M., Bazan J.F., Fletterick R.J.;
RT   "Characterization of the catalytic residues of the tobacco etch virus
RT   49-kDa proteinase.";
RL   Virology 172:302-310(1989).
RN   [6]
RP   ACTIVE SITES OF P1 PROTEINASE, AND MUTAGENESIS OF HIS-214 AND SER-256.
RX   PubMed=1962435; DOI=10.1016/0042-6822(91)90522-d;
RA   Verchot J., Koonin E.V., Carrington J.C.;
RT   "The 35-kDa protein from the N-terminus of the potyviral polyprotein
RT   functions as a third virus-encoded proteinase.";
RL   Virology 185:527-535(1991).
RN   [7]
RP   FUNCTION OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF PHE-314
RP   AND LYS-358.
RX   PubMed=9880030; DOI=10.1099/0022-1317-79-12-3119;
RA   Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C.,
RA   Baker J., Pirone T.P.;
RT   "Mutations in the potyvirus helper component protein: effects on
RT   interactions with virions and aphid stylets.";
RL   J. Gen. Virol. 79:3119-3122(1998).
RN   [8]
RP   FUNCTION OF HELPER COMPONENT PROTEINASE.
RX   PubMed=11414807; DOI=10.1006/viro.2001.0901;
RA   Kasschau K.D., Carrington J.C.;
RT   "Long-distance movement and replication maintenance functions
RT   correlate with silencing suppression activity of potyviral HC-Pro.";
RL   Virology 285:71-81(2001).
RN   [9]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2038-2794, SUBUNIT, AND
RP   DISULFIDE BOND.
RX   PubMed=12377789; DOI=10.1074/jbc.m207224200;
RA   Phan J., Zdanov A., Evdokimov A.G., Tropea J.E., Peters H.K. III,
RA   Kapust R.B., Li M., Wlodawer A., Waugh D.S.;
RT   "Structural basis for the substrate specificity of tobacco etch virus
RT   protease.";
RL   J. Biol. Chem. 277:50564-50572(2002).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2038-2279, SUBUNIT, DISULFIDE
RP   BOND, AND ACTIVE SITES OF NUCLEAR INCLUSION PROTEIN A.
RX   PubMed=15919091; DOI=10.1016/j.jmb.2005.04.013;
RA   Nunn C.M., Jeeves M., Cliff M.J., Urquhart G.T., George R.R.,
RA   Chao L.H., Tscuchia Y., Djordjevic S.;
RT   "Crystal structure of tobacco etch virus protease shows the protein C
RT   terminus bound within the active site.";
RL   J. Mol. Biol. 350:145-155(2005).
CC   -!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in
CC       the regulation of viral RNA amplification.
CC   -!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC   -!- FUNCTION: Helper component proteinase: required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a
CC       Gly-Gly dipeptide at its own C-terminus. Interacts with virions
CC       and aphid stylets. Acts as a suppressor of RNA-mediated gene
CC       silencing, also known as post-transcriptional gene silencing
CC       (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. May have RNA-binding activity.
CC   -!- FUNCTION: Cytoplasmic inclusion protein: has helicase activity. It
CC       may be involved in replication.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus
CC       replication. {ECO:0000250, ECO:0000269|PubMed:11414807,
CC       ECO:0000269|PubMed:9880030}.
CC   -!- FUNCTION: Nuclear inclusion protein A: has RNA-binding and
CC       proteolytic activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that
CC         vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-
CC         Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The
CC         natural substrate is the viral polyprotein, but other proteins
CC         and oligopeptides containing the appropriate consensus sequence
CC         are also cleaved.; EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus,
CC         commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
CC         processing of the potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBUNIT: Nuclear inclusion protein A protease is a dimer;
CC       disulfide-linked. {ECO:0000269|PubMed:12377789,
CC       ECO:0000269|PubMed:15919091}.
CC   -!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=P04517-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CK09-1; Sequence=External;
CC         Note=Produced by -1 ribosomal frameshifting in P3 ORF.;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved
CC       in interaction with stylets. The central part is involved in
CC       interaction with virions and the C-terminus is involved in cell-to
CC       cell movement of the virus.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently
CC       attached to the 5'-end of the genomic RNA. This uridylylated form
CC       acts as a nucleotide-peptide primer for the polymerase (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo
CC       post-translational proteolytic processing. Genome polyprotein is
CC       processed by NIa-pro, P1 and HC-pro proteinases resulting in the
CC       production of at least ten individual proteins. P3N-PIPO
CC       polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC       the production of three individual proteins. The P1 proteinase and
CC       the HC-pro cleave only their respective C-termini
CC       autocatalytically. 6K1 is essential for proper proteolytic
CC       separation of P3 from CI (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; M15239; AAA47910.1; -; Genomic_RNA.
DR   EMBL; M11458; AAA47909.1; -; Genomic_RNA.
DR   EMBL; M11216; AAA47908.1; ALT_SEQ; Genomic_RNA.
DR   PIR; A04207; GNBVEV.
DR   RefSeq; NP_062908.1; NC_001555.1. [P04517-1]
DR   PDB; 1LVB; X-ray; 2.20 A; A/B=2038-2273, C/D=2785-2794.
DR   PDB; 1LVM; X-ray; 1.80 A; A/B=2038-2258, C/D=2786-2794, E=2267-2273.
DR   PDB; 1Q31; X-ray; 2.70 A; A/B=2038-2279.
DR   PDBsum; 1LVB; -.
DR   PDBsum; 1LVM; -.
DR   PDBsum; 1Q31; -.
DR   SMR; P04517; -.
DR   MEROPS; C04.004; -.
DR   PRIDE; P04517; -.
DR   GeneID; 1502321; -.
DR   KEGG; vg:1502321; -.
DR   EvolutionaryTrace; P04517; -.
DR   PMAP-CutDB; P04517; -.
DR   Proteomes; UP000007404; Genome.
DR   Proteomes; UP000201712; Genome.
DR   GO; GO:0019029; C:helical viral capsid; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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; 3.90.70.150; -; 1.
DR   InterPro; IPR011492; DEAD_Flavivir.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Capsid protein; Complete proteome;
KW   Covalent protein-RNA linkage; Disulfide bond; Helical capsid protein;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; Ribosomal frameshifting;
KW   RNA-directed RNA polymerase; Serine protease;
KW   Suppressor of RNA silencing; Thiol protease; Transferase;
KW   Viral RNA replication; Virion.
FT   CHAIN         1   3054       Genome polyprotein.
FT                                /FTId=PRO_0000420026.
FT   CHAIN         1    304       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040450.
FT   CHAIN       305    763       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040451.
FT   CHAIN       764   1110       Protein P3. {ECO:0000250}.
FT                                /FTId=PRO_0000040452.
FT   CHAIN      1111   1163       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040453.
FT   CHAIN      1164   1796       Cytoplasmic inclusion protein.
FT                                /FTId=PRO_0000040454.
FT   CHAIN      1797   1849       6 kDa protein 2.
FT                                /FTId=PRO_0000040455.
FT   CHAIN      1850   2037       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040456.
FT   CHAIN      2038   2279       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040457.
FT   CHAIN      2280   2791       Nuclear inclusion protein B.
FT                                /FTId=PRO_0000040458.
FT   CHAIN      2792   3054       Capsid protein.
FT                                /FTId=PRO_0000040459.
FT   DOMAIN      163    304       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      641    763       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1234   1386       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1401   1564       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2038   2255       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2521   2641       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1247   1254       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       358    361       Involved in interaction with stylet and
FT                                aphid transmission.
FT   MOTIF       615    617       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1336   1339       DECH box.
FT   MOTIF      1889   1896       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    214    214       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    223    223       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    256    256       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    649    649       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    722    722       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2083   2083       For nuclear inclusion protein A activity.
FT   ACT_SITE   2118   2118       For nuclear inclusion protein A activity.
FT   ACT_SITE   2188   2188       For nuclear inclusion protein A activity.
FT   SITE        304    305       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        763    764       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1110   1111       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1163   1164       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1796   1797       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1849   1850       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2037   2038       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2279   2280       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2791   2792       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1911   1911       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
FT   DISULFID   2167   2167       Interchain. {ECO:0000269|PubMed:12377789,
FT                                ECO:0000269|PubMed:15919091}.
FT   MUTAGEN     214    214       H->A: Complete loss of proteolytic
FT                                activity of P1 proteinase.
FT                                {ECO:0000269|PubMed:1962435}.
FT   MUTAGEN     256    256       S->A: Complete loss of proteolytic
FT                                activity of P1 proteinase.
FT                                {ECO:0000269|PubMed:1962435}.
FT   MUTAGEN     314    314       F->L: Complete loss of aphid
FT                                transmission.
FT                                {ECO:0000269|PubMed:9880030}.
FT   MUTAGEN     358    358       K->E: Complete loss of interaction with
FT                                stylet and aphid transmission; no effect
FT                                on virion binding.
FT                                {ECO:0000269|PubMed:9880030}.
FT   MUTAGEN     610    610       S->T: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     619    619       H->S: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     625    625       S->T: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     627    627       D->E: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     632    632       D->E: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     649    649       C->S: Complete loss of proteolytic
FT                                activity of HC-pro.
FT                                {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     675    675       D->E: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     689    689       D->E: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     694    694       C->S: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     698    698       S->T: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     715    715       D->E: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     716    716       H->S: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     722    722       H->S: Complete loss of proteolytic
FT                                activity of HC-pro.
FT                                {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     725    725       D->E: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     726    726       S->T: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     729    729       S->T: No effect on proteolytic activity
FT                                of HC-pro.
FT   MUTAGEN     735    735       H->S: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     743    743       S->T: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   MUTAGEN     755    755       S->T: No effect on proteolytic activity
FT                                of HC-pro. {ECO:0000269|PubMed:2688301}.
FT   HELIX      2038   2040       {ECO:0000244|PDB:1LVM}.
FT   HELIX      2049   2052       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2055   2062       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2065   2074       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2077   2080       {ECO:0000244|PDB:1LVM}.
FT   HELIX      2082   2086       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2089   2096       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2099   2104       {ECO:0000244|PDB:1LVM}.
FT   HELIX      2106   2108       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2109   2113       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2120   2123       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2145   2152       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2154   2157       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2159   2162       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2169   2171       {ECO:0000244|PDB:1LVM}.
FT   TURN       2172   2175       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2176   2179       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2191   2194       {ECO:0000244|PDB:1LVM}.
FT   TURN       2195   2197       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2200   2208       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2209   2211       {ECO:0000244|PDB:1Q31}.
FT   STRAND     2213   2218       {ECO:0000244|PDB:1LVM}.
FT   HELIX      2223   2228       {ECO:0000244|PDB:1LVM}.
FT   HELIX      2230   2232       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2235   2238       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2243   2248       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2251   2256       {ECO:0000244|PDB:1LVM}.
FT   STRAND     2276   2278       {ECO:0000244|PDB:1Q31}.
FT   STRAND     2788   2790       {ECO:0000244|PDB:1LVM}.
SQ   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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