POLG_TVMV
ID POLG_TVMV Reviewed; 3023 AA.
AC P09814; Q84898; Q84899; Q84900; Q84901; Q84902;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=P1 proteinase;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P04517};
DE AltName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Helper component proteinase;
DE Short=HC-pro;
DE EC=3.4.22.45 {ECO:0000250|UniProtKB:P04517};
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 vein mottling virus (TVMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12228;
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH NCBI_TaxID=3618; Rumex.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3737407; DOI=10.1093/nar/14.13.5417;
RA Domier L.L., Franklin K.M., Shahabuddin M., Hellmann G.M., Overmeyer J.H.,
RA Hiremath S.T., Siaw M.F.E., Lomonossoff G.P., Shaw J.G., Rhoads R.E.;
RT "The nucleotide sequence of tobacco vein mottling virus RNA.";
RL Nucleic Acids Res. 14:5417-5430(1986).
RN [2]
RP SEQUENCE REVISION.
RA Shaw J.G.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1874-1888, COVALENT RNA LINKAGE AT TYR-1878 (VPG), AND
RP URIDYLYLATION AT TYR-1878.
RX PubMed=1702164; DOI=10.1128/jvi.65.1.511-513.1991;
RA Murphy J.F., Rychlik W., Rhoads R.E., Hunt A.G., Shaw J.G.;
RT "A tyrosine residue in the small nuclear inclusion protein of tobacco vein
RT mottling virus links the VPg to the viral RNA.";
RL J. Virol. 65:511-513(1991).
RN [4]
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 [5]
RP FUNCTION (6 KDA PROTEIN 2), AND SUBCELLULAR LOCATION (6 KDA PROTEIN 2).
RX PubMed=19906931; DOI=10.1128/jvi.01824-09;
RA Wei T., Huang T.S., McNeil J., Laliberte J.F., Hong J., Nelson R.S.,
RA Wang A.;
RT "Sequential recruitment of the endoplasmic reticulum and chloroplasts for
RT plant potyvirus replication.";
RL J. Virol. 84:799-809(2010).
RN [6]
RP FUNCTION (6 KDA PROTEIN 2), DOMAIN (6 KDA PROTEIN 2), MUTAGENESIS OF
RP 1796-GLY--GLY-1800, AND SUBCELLULAR LOCATION (6 KDA PROTEIN 2).
RX PubMed=30150314; DOI=10.1105/tpc.18.00281;
RA Cabanillas D.G., Jiang J., Movahed N., Germain H., Yamaji Y., Zheng H.,
RA Laliberte J.F.;
RT "Turnip Mosaic Virus Uses the SNARE Protein VTI11 in an Unconventional
RT Route for Replication Vesicle Trafficking.";
RL Plant Cell 30:2594-2615(2018).
CC -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC dipeptide at its own C-terminus. Interacts with virions and aphid
CC stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC known as post-transcriptional gene silencing (PTGS), a mechanism of
CC plant viral defense that limits the accumulation of viral RNAs. May
CC have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It
CC may be involved in replication.
CC -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P13529}.
CC -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000269|PubMed:19906931}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
CC -!- FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-
CC cell and systemis movement, encapsidation of the viral RNA and in the
CC regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC potyviral polyprotein.; EC=3.4.22.45;
CC Evidence={ECO:0000250|UniProtKB:P04517};
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: [Viral genome-linked protein]: Interacts with host eIF4E
CC protein (via cap-binding region); this interaction mediates the
CC translation of the VPg-viral RNA conjugates (By similarity). Part of a
CC complex that comprises VPg, RNA, host EIF4E and EIF4G; this interaction
CC mediates the translation of the VPg-viral RNA conjugates (By
CC similarity). {ECO:0000250|UniProtKB:P18247}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle.
CC Note=Probably colocalizes with 6K2-induced vesicles associated with
CC host chloroplasts. {ECO:0000250|UniProtKB:P13529}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC {ECO:0000269|PubMed:19906931, ECO:0000269|PubMed:30150314}. Note=6K-
CC induced vesicles associate with host chloroplasts.
CC {ECO:0000269|PubMed:19906931}.
CC -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host nucleus
CC {ECO:0000250|UniProtKB:P21231}. Note=Binds to host plant eIF4E proteins
CC in the host nucleus. {ECO:0000250|UniProtKB:P21231}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=P09814-1; Sequence=Displayed;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK10-1; Sequence=External;
CC -!- DOMAIN: [6 kDa protein 2]: The GxxxG motif is essential for the viral
CC infection. {ECO:0000269|PubMed:30150314}.
CC -!- DOMAIN: [Helper component proteinase]: The N-terminus is involved in
CC interaction with stylets. The central part is involved in interaction
CC with virions and the C-terminus is involved in cell-to cell movement of
CC the virus.
CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase. {ECO:0000269|PubMed:1702164}.
CC -!- PTM: [Genome polyprotein]: Potyviral RNA is expressed as two
CC polyproteins which undergo post-translational proteolytic processing.
CC Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases
CC resulting in the production of at least ten individual proteins. P3N-
CC PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in
CC the production of three individual proteins. The P1 proteinase and the
CC HC-pro cleave only their respective C-termini autocatalytically. 6K1 is
CC essential for proper proteolytic separation of P3 from CI (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; X04083; CAA27720.1; -; Genomic_RNA.
DR PIR; A23647; GNVSTV.
DR RefSeq; NP_056867.1; NC_001768.1. [P09814-1]
DR PDB; 3MMG; X-ray; 1.70 A; A/B=2002-2242, C/D=2753-2760.
DR PDBsum; 3MMG; -.
DR SMR; P09814; -.
DR MEROPS; C04.003; -.
DR MEROPS; C06.001; -.
DR PRIDE; P09814; -.
DR GeneID; 1494056; -.
DR KEGG; vg:1494056; -.
DR Proteomes; UP000007549; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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:0019048; P:modulation by virus of host process; ISS:UniProtKB.
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; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.150; -; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR039560; Potyvirid-P3.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00270; 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 SUPFAM; SSF56672; SSF56672; 1.
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; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Direct protein sequencing; Helical capsid protein; Helicase;
KW Host cytoplasmic vesicle; Host nucleus; Host-virus interaction; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..3023
FT /note="Genome polyprotein"
FT /id="PRO_0000420031"
FT CHAIN 1..274
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040483"
FT CHAIN 275..731
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040484"
FT CHAIN 732..1078
FT /note="Protein P3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040485"
FT CHAIN 1079..1130
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040486"
FT CHAIN 1131..1765
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040487"
FT CHAIN 1766..1818
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040488"
FT CHAIN 1819..2001
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040489"
FT CHAIN 2002..2242
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040490"
FT CHAIN 2243..2758
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040491"
FT CHAIN 2759..3023
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040492"
FT DOMAIN 132..274
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 609..731
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT DOMAIN 1202..1354
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1367..1532
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2002..2218
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 2484..2608
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT MOTIF 325..328
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 583..585
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT MOTIF 1304..1307
FT /note="DEFH box"
FT MOTIF 1796..1800
FT /note="GxxxG motif"
FT /evidence="ECO:0000269|PubMed:30150314"
FT MOTIF 1856..1863
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 192
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 225
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 617
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 690
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 2047
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2082
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 2152
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 1215..1222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 274..275
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 731..732
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 1078..1079
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1130..1131
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1765..1766
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 1818..1819
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2001..2002
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2242..2243
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT SITE 2758..2759
FT /note="Cleavage; by NIa-pro"
FT /evidence="ECO:0000250"
FT MOD_RES 1878
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000269|PubMed:1702164"
FT MOD_RES 1878
FT /note="O-UMP-tyrosine; transient"
FT /evidence="ECO:0000269|PubMed:1702164"
FT MUTAGEN 1796..1800
FT /note="GIGLG->VIGLV: Complete loss of capacity to form
FT vesicles and mislocalization to the Golgi apparatus and
FT plasma membrane."
FT /evidence="ECO:0000269|PubMed:30150314"
FT HELIX 2013..2016
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2019..2026
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2029..2038
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2041..2044
FT /evidence="ECO:0007829|PDB:3MMG"
FT HELIX 2046..2049
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2055..2060
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2063..2069
FT /evidence="ECO:0007829|PDB:3MMG"
FT HELIX 2070..2072
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2075..2077
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2080..2082
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2084..2087
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2110..2117
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2122..2130
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2138..2143
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2155..2158
FT /evidence="ECO:0007829|PDB:3MMG"
FT TURN 2159..2161
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2164..2172
FT /evidence="ECO:0007829|PDB:3MMG"
FT TURN 2173..2175
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2178..2182
FT /evidence="ECO:0007829|PDB:3MMG"
FT HELIX 2187..2191
FT /evidence="ECO:0007829|PDB:3MMG"
FT HELIX 2206..2208
FT /evidence="ECO:0007829|PDB:3MMG"
FT STRAND 2754..2757
FT /evidence="ECO:0007829|PDB:3MMG"
SQ SEQUENCE 3023 AA; 342285 MW; 299FDED15C0E5B87 CRC64;
MAATMIFGSF THDLLGKAMS TIHSAVTAEK DIFSSIKERL ERKRHGKICR MKNGSIYIKA
ASSTKVEKIN AAAKKLADDK AAFLKAQPTI VDKIIVNEKI QVVEAEEVHK REDVQTVFFK
KTKKRAPKLR ATCSSSGLDN LYNAVANIAK ASSLRVEVIH KKRVCGEFKQ TRFGRALFID
VAHAKGHRRR IDCRMHRREQ RTMHMFMRKT TKTEVRSKHL RKGDSGIVLL TQKIKGHLSG
VRDEFFIVRG TCDDSLLEAR ARFSQSITLR ATHFSTGDIF WKGFNASFQE QKAIGLDHTC
TSDLPVEACG HVAALMCQSL FPCGKITCKR CIANLSNLDF DTFSELQGDR AMRILDVMRA
RFPSFTHTIR FLHDLFTQRR VTNPNTAAFR EILRLIGDRN EAPFAHVNRL NEILLLGSKA
NPDSLAKASD SLLELARYLN NRTENIRNGS LKHFRNKISS KAHSNLALSC DNQLDQNGNF
LWGLAGIAAK RFLNNYFETI DPEQGYDKYV IRKNPNGERK LAIGNFIIST NLEKLRDQLE
GESIARVGIT EECVSRKDGN YRYPCCCVTL EDGSPMYSEL KMPTKNHLVI GNSGDPKYLD
LPGEISNLMY IAKEGYCYIN IFLAMLVNVD EANAKDFTKR VRDESVQKLG KWPSLIDVAT
ECALLSTYYP AAASAELPRL LVDHAQKTIH VVDSYGSLNT GYHILKANTV SQLEKFASNT
LESPMAQYKV GGLVYSENND ASAVKALTQA IFRPDVLSEL IEKEPYLMVF ALVSPGILMA
MSNSGALEFG ISKWISSDHS LVRMASILKT LASKVSVADT LALQKHIMRQ NANFLCGELI
NGFQKKKSYT HATRFLLMIS EENEMDDPVL NAGYRVLEAS SHEIMEKTYL ALLETSWSDL
SLYGKFKSIW FTRKHFGRYK AELFPKEQTD LQGRYSNSLR FHYQSTLKRL RNKGSLCRER
FLESISSARR RTTCAVFSLL HKAFPDVLKF INTLVIVSLS MQIYYMLVAI IHEHRAAKIK
SAQLEERVLE DKTMLLYDDF KAKLPEGSFE EFLEYTRQRD KEVYEYLMME TTEIVEFQAK
NTGQASLERI IAFVSLTLML FDNERSDCVY KILTKFKGIL GSVENNVRFQ SLDTIVPTQE
EKNMVIDFEL DSDTAHTPQM QEQTFSDWWS NQIANNRVVP HYRTEGYFMQ FTRNTASAVS
HQIAHNEHKD IILMGAVGSG KSTGLPTNLC KFGGVLLLEP TRPLAENVTK QMRGSPFFAS
PTLRMRNLST FGSSPITVMT TGFALHFFAN NVKEFDRYQF IIFDEFHVLD SNAIAFRNLC
HEYSYNGKII KVSATPPGRE CDLTTQYPVE LLIEEQLSLR DFVDAQGTDA HADVVKKGDN
ILVYVASYNE VDQLSKMLNE RGFLVTKVDG RTMKLGGVEI ITKGSSIKKH FIVATNIIEN
GVTLDVDVVV DFGLKVVPNL DSDNRLVSYC KIPISLGERI QRFGRVGRNK PGVALRIGET
IKGLVEIPSM IATEAAFLCF VYGLPVTTQN VSTSILSQVS VRQARVMCQF ELPIFYTAHL
VRYDGAMHPA IHNALKRFKL RDSEINLNTL AIPTSSSKTW YTGKCYKQLV GRLDIPDEIK
IPFYTKEVPE KVPEQIWDVM VKFSSDAGFG RMTSAAACKV AYTLQTDIHS IQRTVQIIDR
LLENEMKKRN HFNLVVNQSC SSHFMSLSSI MASLRAHYAK NHTGQNIEIL QKAKAQLLEF
SNLAIDPSTT EALRDFGYLE AVRFQSESEM ARGLKLSGHW KWSLISRDLI VVSGVGIGLG
CMLWQFFKEK MHEPVKFQGK SRRRLQFRKA RDDKMGYIMH GEGDTIEHFF GAAYTKKGKS
KGKTHGAGTK AHKFVNMYGV SPDEYSYVRY LDPVTGATLD ESPMTDLNIV QEHFGEIRRE
AILADAMSPQ QRNKGIQAYF VRNSTMPILK VDLTPHIPLK VCESNNIAGF PEREGELRRT
GPTETLPFDA LPPEKQEVAF ESKALLKGVR DFNPISACVW LLENSSDGHS ERLFGIGFGP
YIIANQHLFR RNNGELTIKT MHGEFKVKNS TQLQMKPVEG RDIIVIKMAK DFPPFPQKLK
FRQPTIKDRV CMVSTNFQQK SVSSLVSESS HIVHKEDTSF WQHWITTKDG QCGSPLVSII
DGNILGIHSL THTTNGSNYF VEFPEKFVAT YLDAADGWCK NWKFNADKIS WGSFTLVEDA
PEDDFMAKKT VAAIMDDLVR TQGEKRKWML EAAHTNIQPV AHLQSQLVTK HIVKGRCKMF
ALYLQENADA RDFFKSFMGA YGPSHLNKEA YIKDIMKYSK QIVVGSVDCD TFESSLKVLS
RKMKEWGFEN LEYVTDEQTI KNALNMDAAV GALYSGKKKQ YFEDLSDDAV ANLVQKSCLR
LFKNKLGVWN GSLKAELRPF EKLIENKTRT FTAAPIETLL GGKVCVDDFN NHFYSKHIQC
PWSVGMTKFY GGWNELLGKL PDGWVYCDAD GSQFDSSLSP YLINAVLRLR LSSMEEWDVG
QKMLQNLYTE IVYTPISTPD GTIVKKFKGN NSGQPSTVVD NTLMVVLAMY YALSKLGVDI
NSQEDVCKFF ANGDDLIIAI SPELEHVLDG FQQHFSDLGL NYDFSSRTRD KKELWFMSHR
ALSKDGILIP KLEPERIVSI LEWDRSAEPH HRLEAICASM IEAWGYTDLL QNIRRFYKWT
IEQEPYRSLA EQGLAPYLSE VALRRLYTSQ IATDNELTDY YKEILANNEF LRETVRFQSD
TVDAGKDKAR DQKLADKPTL AIDRTKDKDV NTGTSGTFSI PRLKKAAMNM KLPKVGGSSV
VNLDHLLTYK PAQEFVVNTR ATHSQFKAWH TNVMAELELN EEQMKIVLNG FMIWCIENGT
SPNISGVWTM MDGDEQVEYP IEPMVKHANP SLRQIMKHFS NLAEAYIRMR NSEQVYIPRY
GLQRGLVDRN LAPFAFDFFE VNGATPVRAR EAHAQMKAAA LRNSQQRMFC LDGSVSGQEE
NTERHTVDDV NAQMHHLLGV KGV
