MCEL_VACCW
ID MCEL_VACCW Reviewed; 844 AA.
AC P04298; Q76ZS6;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=mRNA-capping enzyme catalytic subunit;
DE AltName: Full=Virus termination factor large subunit;
DE Short=VTF large subunit;
DE AltName: Full=mRNA-capping enzyme 97 kDa subunit;
DE AltName: Full=mRNA-capping enzyme D1 subunit;
DE AltName: Full=mRNA-capping enzyme large subunit;
DE Includes:
DE RecName: Full=Polynucleotide 5'-triphosphatase;
DE EC=3.1.3.33;
DE AltName: Full=mRNA 5'-triphosphatase;
DE Short=TPase;
DE Includes:
DE RecName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50;
DE AltName: Full=GTP--RNA guanylyltransferase;
DE Short=GTase;
DE Includes:
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE EC=2.1.1.56;
DE AltName: Full=mRNA cap methyltransferase;
GN OrderedLocusNames=VACWR106; ORFNames=D1R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT fragment.";
RL Virology 153:96-112(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP COFACTOR.
RX PubMed=2164022; DOI=10.1016/s0021-9258(19)38494-7;
RA Shuman S.;
RT "Catalytic activity of vaccinia mRNA capping enzyme subunits coexpressed in
RT Escherichia coli.";
RL J. Biol. Chem. 265:11960-11966(1990).
RN [4]
RP INTERACTION WITH SMALL SUBUNIT, AND PROTEIN SEQUENCE OF 1-20 AND 498-517.
RX PubMed=2161527; DOI=10.1073/pnas.87.11.4023;
RA Guo P., Moss B.;
RT "Interaction and mutual stabilization of the two subunits of vaccinia virus
RT mRNA capping enzyme coexpressed in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4023-4027(1990).
RN [5]
RP DOMAIN METHYLTRANSFERASE.
RX PubMed=7929111; DOI=10.1016/s0021-9258(19)51108-5;
RA Mao X., Shuman S.;
RT "Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus
RT capping enzyme D1 subunit is stimulated by the D12 subunit. Identification
RT of amino acid residues in the D1 protein required for subunit association
RT and methyl group transfer.";
RL J. Biol. Chem. 269:24472-24479(1994).
RN [6]
RP ACTIVE SITE OF TRIPHOSPHATASE ACTIVITY, AND MUTAGENESIS OF 77-ARG--LYS-79;
RP 135-LYS-LYS-136; 160-PHE-LYS-161; 192-GLU--GLU-194; LYS-260 AND
RP 524-LYS--GLY-526.
RX PubMed=8709242; DOI=10.1128/jvi.70.9.6162-6168.1996;
RA Yu L., Shuman S.;
RT "Mutational analysis of the RNA triphosphatase component of vaccinia virus
RT mRNA capping enzyme.";
RL J. Virol. 70:6162-6168(1996).
RN [7]
RP CHARACTERIZATION OF TRIPHOSPHATASE ACTIVITY, AND MUTAGENESIS OF LYS-107;
RP GLU-126; ASP-159 AND LYS-161.
RX PubMed=12726733; DOI=10.1016/s0042-6822(03)00002-3;
RA Gong C., Shuman S.;
RT "Mapping the active site of vaccinia virus RNA triphosphatase.";
RL Virology 309:125-134(2003).
RN [8]
RP FUNCTION.
RC STRAIN=IHDW, and mutant Dts36;
RX PubMed=18295814; DOI=10.1016/j.virol.2008.01.028;
RA Shatzer A.N., Kato S.E., Condit R.C.;
RT "Phenotypic analysis of a temperature sensitive mutant in the large subunit
RT of the vaccinia virus mRNA capping enzyme.";
RL Virology 375:236-252(2008).
RN [9]
RP FUNCTION.
RX PubMed=18455214; DOI=10.1016/j.virol.2008.03.031;
RA Christen L.A., Piacente S., Mohamed M.R., Niles E.G.;
RT "Vaccinia virus early gene transcription termination factors VTF and Rap94
RT interact with the U9 termination motif in the nascent RNA in a
RT transcription ternary complex.";
RL Virology 376:225-235(2008).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASN-570;
RP LYS-573; LYS-607; TYR-608; ASP-676; PHE-679; HIS-682 AND GLU-763.
RX PubMed=18256245; DOI=10.1261/rna.928208;
RA Zheng S., Shuman S.;
RT "Structure-function analysis of vaccinia virus mRNA cap (guanine-N7)
RT methyltransferase.";
RL RNA 14:696-705(2008).
RN [11] {ECO:0007744|PDB:2VDW}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 545-844 IN COMPLEX WITH ADOHCY AND
RP THE REGULATORY SUBUNIT.
RX PubMed=17989694; DOI=10.1038/sj.emboj.7601912;
RA De la Pena M., Kyrieleis O.J., Cusack S.;
RT "Structural insights into the mechanism and evolution of the vaccinia virus
RT mRNA cap N7 methyl-transferase.";
RL EMBO J. 26:4913-4925(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GTP AND
RP S-ADENOSYL-L-HOMOCYSTEINE, AND COFACTOR.
RX PubMed=24607143; DOI=10.1016/j.str.2013.12.014;
RA Kyrieleis O.J., Chang J., de la Pena M., Shuman S., Cusack S.;
RT "Crystal structure of vaccinia virus mRNA capping enzyme provides insights
RT into the mechanism and evolution of the capping apparatus.";
RL Structure 22:452-465(2014).
CC -!- FUNCTION: Catalytic subunit of the mRNA capping enzyme which catalyzes
CC three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is
CC hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate
CC RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap
CC is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA
CC capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to
CC the first transcribed nucleotide (cap 0 structure), whereas the
CC polymerase associated VP39 is responsible for a second methylation at
CC the 2'-O position of the ribose (cap 1 structure).
CC -!- FUNCTION: The heterodimeric enzyme is also involved in early viral gene
CC transcription termination and intermediate viral gene transcription
CC initiation. Early gene transcription termination requires the
CC termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94
CC subunit of the viral RNA polymerase, as well as the presence of a
CC specific termination motif. Binds, together with RAP94, to the
CC termination motif 5'-UUUUUNU-3' in the nascent early mRNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a
CC 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:2164022, ECO:0000305|PubMed:24607143};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for GpppA {ECO:0000269|PubMed:18256245};
CC Note=A-570 and A-763 mutants have 3-fold and 10-fold higher Km values
CC for GpppA.;
CC -!- SUBUNIT: Heterodimer of a catalytic and a regulatory subunit. Intrinsic
CC methyltransferase activity of the catalytic subunit is weak and needs
CC to be stimulated 30- to 50-fold by the regulatory subunit, which is
CC itself catalytically inert. {ECO:0000269|PubMed:17989694}.
CC -!- INTERACTION:
CC P04298; P04318: VACWR117; NbExp=3; IntAct=EBI-16095746, EBI-16095776;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and
CC other proteins required to synthesize early mRNAs are packaged within
CC the virion core along with the DNA genome.
CC -!- DOMAIN: The N-terminus contains the triphosphatase and
CC guanylyltransferase domains, whereas the C-terminus contains the
CC methyltransferase domain. The N-terminus is involved in binding to the
CC termination motif 5'-UUUUUNU-3' in the nascent mRNA.
CC {ECO:0000269|PubMed:7929111}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC guanylyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class I-like SAM-
CC binding methyltransferase superfamily. mRNA cap 0 methyltransferase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
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DR EMBL; M15058; AAA48253.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89385.1; -; Genomic_DNA.
DR PIR; A03872; QQVZ1.
DR RefSeq; YP_232988.1; NC_006998.1.
DR PDB; 2VDW; X-ray; 2.70 A; A/C/E/G=545-844.
DR PDB; 4CKB; X-ray; 2.80 A; A/D=1-844.
DR PDB; 4CKC; X-ray; 2.90 A; A/D=1-844.
DR PDB; 4CKE; X-ray; 2.90 A; A/D=1-844.
DR PDB; 6RIE; EM; 3.10 A; O=1-844.
DR PDBsum; 2VDW; -.
DR PDBsum; 4CKB; -.
DR PDBsum; 4CKC; -.
DR PDBsum; 4CKE; -.
DR PDBsum; 6RIE; -.
DR SMR; P04298; -.
DR DIP; DIP-60664N; -.
DR IntAct; P04298; 1.
DR DNASU; 3707562; -.
DR GeneID; 3707562; -.
DR KEGG; vg:3707562; -.
DR BRENDA; 2.7.7.50; 6591.
DR SABIO-RK; P04298; -.
DR EvolutionaryTrace; P04298; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050355; F:triphosphatase activity; IMP:UniProtKB.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019602; mRNA_cap_ATPase/GuylTrfase_vir.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF10640; Pox_ATPase-GT; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; GTP-binding; Hydrolase; Magnesium;
KW Metal-binding; Methyltransferase; mRNA capping; mRNA processing;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transcription termination; Transferase; Virion.
FT CHAIN 1..844
FT /note="mRNA-capping enzyme catalytic subunit"
FT /id="PRO_0000210124"
FT DOMAIN 516..844
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..539
FT /note="Triphosphatase-guanylyltransferase"
FT ACT_SITE 260
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000255"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24607143"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24607143"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24607143"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24607143"
FT BINDING 549..550
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 569..570
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 573
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 598
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 620
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 678..680
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT SITE 77
FT /note="Essential for RNA triphosphatase activity"
FT SITE 107
FT /note="Essential for RNA triphosphatase activity"
FT SITE 126
FT /note="Essential for RNA triphosphatase activity"
FT SITE 159
FT /note="Essential for RNA triphosphatase activity"
FT SITE 161
FT /note="Essential for RNA triphosphatase activity"
FT SITE 607
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 632
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 682
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 763
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 836
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT VARIANT 705
FT /note="G -> D (in strain: mutant Dts36)"
FT MUTAGEN 77..79
FT /note="RTK->ATA: Almost complete loss of RNA triphosphatase
FT activity, 70% loss of guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:8709242"
FT MUTAGEN 107
FT /note="K->A: Complete loss of triphosphatase activity, no
FT effect on guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12726733"
FT MUTAGEN 126
FT /note="E->A: Complete loss of triphosphatase activity, no
FT effect on guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12726733"
FT MUTAGEN 135..136
FT /note="KK->AA: 70% loss of RNA triphosphatase activity, 40%
FT loss of guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:8709242"
FT MUTAGEN 159
FT /note="D->A: Complete loss of triphosphatase activity, no
FT effect on guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12726733"
FT MUTAGEN 161
FT /note="K->A: Complete loss of triphosphatase activity, no
FT effect on guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12726733"
FT MUTAGEN 192..194
FT /note="EIE->AIA: Complete loss of RNA triphosphatase
FT activity, 50% loss of guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:8709242"
FT MUTAGEN 260
FT /note="K->A: Complete loss of guanylyltransferase activity,
FT no effect on RNA triphosphatase activity."
FT /evidence="ECO:0000269|PubMed:8709242"
FT MUTAGEN 524..526
FT /note="KIG->AIA: 50% loss of RNA triphosphatase activity
FT and 40% loss of guanylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:8709242"
FT MUTAGEN 570
FT /note="N->A: Retains substantial methyltransferase activity
FT in vitro; lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 573
FT /note="K->A: Complete loss of methyltransferase activity;
FT lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 607
FT /note="K->A: Retains substantial methyltransferase activity
FT in vitro; lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 608
FT /note="Y->A: Almost complete loss of methyltransferase
FT activity; lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 676
FT /note="D->A: Complete loss of methyltransferase activity;
FT lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 679
FT /note="F->A: Almost complete loss of methyltransferase
FT activity; lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 682
FT /note="H->A: Complete loss of methyltransferase activity;
FT lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT MUTAGEN 763
FT /note="E->A: Retains substantial methyltransferase activity
FT in vitro; lethal in vivo."
FT /evidence="ECO:0000269|PubMed:18256245"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6RIE"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 58..69
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 103..116
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 154..170
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4CKE"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 205..220
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6RIE"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4CKB"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 298..318
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:4CKB"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:4CKB"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:6RIE"
FT STRAND 422..432
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 435..445
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:4CKB"
FT TURN 454..457
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 470..484
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 494..502
FT /evidence="ECO:0007829|PDB:4CKB"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6RIE"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 511..522
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 563..580
FT /evidence="ECO:0007829|PDB:2VDW"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:2VDW"
FT TURN 600..604
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 605..610
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 614..621
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 623..636
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 659..664
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 672..679
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:2VDW"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 690..700
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 701..712
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:2VDW"
FT TURN 734..736
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 737..741
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 748..752
FT /evidence="ECO:0007829|PDB:2VDW"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 768..777
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 780..787
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 788..793
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 796..800
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 802..805
FT /evidence="ECO:0007829|PDB:2VDW"
FT HELIX 809..823
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:4CKB"
FT HELIX 829..833
FT /evidence="ECO:0007829|PDB:2VDW"
FT STRAND 836..843
FT /evidence="ECO:0007829|PDB:2VDW"
SQ SEQUENCE 844 AA; 96734 MW; 8B9FD3DE836FA6E7 CRC64;
MDANVVSSST IATYIDALAK NASELEQRST AYEINNELEL VFIKPPLITL TNVVNISTIQ
ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID NIVWEKKSLV TENRLHKECL
LRLSTEERHI FLDYKKYGSS IRLELVNLIQ AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI
NHPKSRPNTS LEIEFTPRDN ETVPYDELIK ELTTLSRHIF MASPENVILS PPINAPIKTF
MLPKQDIVGL DLENLYAVTK TDGIPITIRV TSNGLYCYFT HLGYIIRYPV KRIIDSEVVV
FGEAVKDKNW TVYLIKLIEP VNAINDRLEE SKYVESKLVD ICDRIVFKSK KYEGPFTTTS
EVVDMLSTYL PKQPEGVILF YSKGPKSNID FKIKKENTID QTANVVFRYM SSEPIIFGES
SIFVEYKKFS NDKGFPKEYG SGKIVLYNGV NYLNNIYCLE YINTHNEVGI KSVVVPIKFI
AEFLVNGEIL KPRIDKTMKY INSEDYYGNQ HNIIVEHLRD QSIKIGDIFN EDKLSDVGHQ
YANNDKFRLN PEVSYFTNKR TRGPLGILSN YVKTLLISMY CSKTFLDDSN KRKVLAIDFG
NGADLEKYFY GEIALLVATD PDADAIARGN ERYNKLNSGI KTKYYKFDYI QETIRSDTFV
SSVREVFYFG KFNIIDWQFA IHYSFHPRHY ATVMNNLSEL TASGGKVLIT TMDGDKLSKL
TDKKTFIIHK NLPSSENYMS VEKIADDRIV VYNPSTMSTP MTEYIIKKND IVRVFNEYGF
VLVDNVDFAT IIERSKKFIN GASTMEDRPS TRNFFELNRG AIKCEGLDVE DLLSYYVVYV
FSKR
