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 24-JAN-2024, entry version 122. 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=3.6.1.74 {ECO:0000269|PubMed:12726733, ECO:0000269|PubMed:8709242}; 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 {ECO:0000269|PubMed:18256245}; DE AltName: Full=mRNA cap methyltransferase; GN Name=OPG113; 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, 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, AND CATALYTIC ACTIVITY. 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, MUTAGENESIS OF LYS-107; RP GLU-126; ASP-159 AND LYS-161, AND CATALYTIC ACTIVITY. 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, MUTAGENESIS OF ASN-570; LYS-573; RP LYS-607; TYR-608; ASP-676; PHE-679; HIS-682 AND GLU-763, AND CATALYTIC RP ACTIVITY. 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 methyltransferase OPG102 is responsible for a second methylation at the CC 2'-O position of the ribose (cap 1 structure). Also involved in early CC viral gene transcription termination and intermediate viral gene CC transcription initiation. Early gene transcription termination requires CC the termination factor VTF, the DNA-dependent ATPase NPH-I/OPG123 and CC the RAP94/OPG109 subunit of the viral RNA polymerase, as well as the CC presence of a specific termination motif. Binds, together with CC RAP94/OPG109, to the termination motif 5'-UUUUUNU-3' in the nascent CC early mRNA. {ECO:0000269|PubMed:18256245, ECO:0000269|PubMed:18295814, CC ECO:0000269|PubMed:18455214}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end CC diphospho-ribonucleoside in mRNA + H(+) + phosphate; CC Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; CC Evidence={ECO:0000269|PubMed:12726733, ECO:0000269|PubMed:8709242}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; CC Evidence={ECO:0000269|PubMed:12726733, ECO:0000269|PubMed:8709242}; 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; CC Evidence={ECO:0000269|PubMed:18256245}; 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: Forms a heterodimer with the regulatory subunit OPG124. CC {ECO:0000269|PubMed:17989694}. CC -!- INTERACTION: CC P04298; P04318: OPG124; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-4890; -. 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:0044423; C:virion component; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0050355; F:inorganic triphosphate phosphatase activity; IMP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IMP:UniProtKB. DR GO; GO:0140818; F:mRNA 5'-phosphatase activity; IEA:RHEA. 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:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.830; -; 1. DR Gene3D; 3.20.100.20; -; 1. DR Gene3D; 3.30.470.140; -; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR048425; MCEL_GT_NTPase. DR InterPro; IPR048426; MCEL_GT_OB. DR InterPro; IPR046429; MCEL_NTPase_sf. DR InterPro; IPR046428; MCEL_OB_dom_sf. DR InterPro; IPR019602; MCEL_TPase. DR InterPro; IPR046430; MCEL_TPase_sf. DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom. DR InterPro; IPR039753; RG7MT1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1. DR PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1. DR Pfam; PF21004; MCEL_GT_NTPase; 1. DR Pfam; PF21005; MCEL_GT_OB; 1. DR Pfam; PF10640; MCEL_TPase; 1. DR Pfam; PF03291; mRNA_G-N7_MeTrfase; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 //