AGLB3_ARCFU
ID AGLB3_ARCFU Reviewed; 868 AA.
AC O29867;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 3;
DE EC=2.4.99.21 {ECO:0000269|PubMed:24127570, ECO:0000269|PubMed:27997792};
DE AltName: Full=Archaeal glycosylation protein B;
DE Short=AglB-L;
DE Short=AglB-Long;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB3; OrderedLocusNames=AF_0380;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE.
RX PubMed=27015803; DOI=10.1074/jbc.m115.713156;
RA Taguchi Y., Fujinami D., Kohda D.;
RT "Comparative analysis of archaeal lipid-linked oligosaccharides that serve
RT as oligosaccharide donors for Asn glycosylation.";
RL J. Biol. Chem. 291:11042-11054(2016).
RN [3] {ECO:0007744|PDB:3WAI}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 500-868.
RX PubMed=23815857; DOI=10.1186/1472-6807-13-11;
RA Matsumoto S., Shimada A., Kohda D.;
RT "Crystal structure of the C-terminal globular domain of the third paralog
RT of the Archaeoglobus fulgidus oligosaccharyltransferases.";
RL BMC Struct. Biol. 13:11-11(2013).
RN [4] {ECO:0007744|PDB:3WAJ, ECO:0007744|PDB:3WAK}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MANGANESE, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF ASP-47; HIS-81; ASP-161; HIS-162; HIS-163;
RP GLU-360 AND ARG-426.
RX PubMed=24127570; DOI=10.1073/pnas.1309777110;
RA Matsumoto S., Shimada A., Nyirenda J., Igura M., Kawano Y., Kohda D.;
RT "Crystal structures of an archaeal oligosaccharyltransferase provide
RT insights into the catalytic cycle of N-linked protein glycosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17868-17873(2013).
RN [5] {ECO:0007744|PDB:5GMY}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP ACCEPTOR PEPTIDE, AND CATALYTIC ACTIVITY.
RX PubMed=27997792; DOI=10.1021/acs.biochem.6b01089;
RA Matsumoto S., Taguchi Y., Shimada A., Igura M., Kohda D.;
RT "Tethering an N-glycosylation sequon-containing peptide creates a
RT catalytically competent oligosaccharyltransferase complex.";
RL Biochemistry 56:602-611(2017).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (a glucose-linked heptasaccharide composed
CC of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the
CC lipid carrier dolichol-monophosphate to an asparagine residue within an
CC Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first
CC step in protein N-glycosylation. {ECO:0000269|PubMed:24127570,
CC ECO:0000269|PubMed:27015803, ECO:0000269|PubMed:27997792}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an archaeal dolichyl phosphooligosaccharide + [protein]-L-
CC asparagine = an archaeal dolichyl phosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.; EC=2.4.99.21;
CC Evidence={ECO:0000269|PubMed:24127570, ECO:0000269|PubMed:27997792};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24127570};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24127570};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24127570};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:24127570}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2EMT4};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24127570}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000305|PubMed:24127570}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; AE000782; AAB90856.1; -; Genomic_DNA.
DR PIR; D69297; D69297.
DR RefSeq; WP_010877887.1; NC_000917.1.
DR PDB; 3WAI; X-ray; 1.90 A; A=500-868.
DR PDB; 3WAJ; X-ray; 2.50 A; A=1-868.
DR PDB; 3WAK; X-ray; 3.41 A; A=1-868.
DR PDB; 5GMY; X-ray; 3.50 A; A=1-868.
DR PDB; 7E9S; X-ray; 2.70 A; A=1-868.
DR PDBsum; 3WAI; -.
DR PDBsum; 3WAJ; -.
DR PDBsum; 3WAK; -.
DR PDBsum; 5GMY; -.
DR PDBsum; 7E9S; -.
DR AlphaFoldDB; O29867; -.
DR SMR; O29867; -.
DR STRING; 224325.AF_0380; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR EnsemblBacteria; AAB90856; AAB90856; AF_0380.
DR GeneID; 24793919; -.
DR KEGG; afu:AF_0380; -.
DR eggNOG; arCOG02043; Archaea.
DR HOGENOM; CLU_008803_0_0_2; -.
DR OMA; NDHHIWE; -.
DR OrthoDB; 5183at2157; -.
DR PhylomeDB; O29867; -.
DR BRENDA; 2.4.99.18; 414.
DR BRENDA; 2.4.99.21; 414.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR DisProt; DP01200; -.
DR InterPro; IPR041154; AglB_P1.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR026410; OlisacTrfase_arch.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF18079; AglB_L1; 1.
DR Pfam; PF02516; STT3; 1.
DR TIGRFAMs; TIGR04154; archaeo_STT3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycosyltransferase; Magnesium; Manganese;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..868
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 3"
FT /id="PRO_0000445596"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 37..101
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 102..131
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 132..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 134..153
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 154..162
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 185..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 200..212
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 213..215
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 239..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 263..279
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 280..303
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 304..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 313..330
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 331..373
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 397..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 405..423
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 424..427
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 428..452
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 453..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24127570"
FT TRANSMEM 469..494
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24127570"
FT TOPO_DOM 495..868
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24127570"
FT REGION 550..552
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:27997792"
FT MOTIF 45..47
FT /note="DXD motif 1"
FT /evidence="ECO:0000305|PubMed:24127570"
FT MOTIF 161..163
FT /note="DXD motif 2"
FT /evidence="ECO:0000305|PubMed:24127570"
FT MOTIF 357..360
FT /note="TIXE motif"
FT /evidence="ECO:0000305|PubMed:24127570"
FT MOTIF 550..554
FT /note="WWDYG motif"
FT /evidence="ECO:0000305|PubMed:23815857"
FT MOTIF 613..622
FT /note="DKi motif"
FT /evidence="ECO:0000305|PubMed:23815857"
FT BINDING 47
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24127570,
FT ECO:0000269|PubMed:27997792, ECO:0007744|PDB:3WAK"
FT BINDING 81
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000305|PubMed:24127570"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24127570,
FT ECO:0000269|PubMed:27997792, ECO:0007744|PDB:3WAK"
FT BINDING 162
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000305|PubMed:24127570"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24127570,
FT ECO:0000269|PubMed:27997792, ECO:0007744|PDB:3WAK"
FT BINDING 426
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000305|PubMed:24127570"
FT SITE 47
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:27997792"
FT SITE 154
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 360
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:27997792"
FT SITE 618
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000269|PubMed:27997792"
FT MUTAGEN 47
FT /note="D->A,N: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 47
FT /note="D->E: Reduces catalytic activity by 80%."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 81
FT /note="H->E: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 161
FT /note="D->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 162
FT /note="H->E: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 163
FT /note="H->A,D: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 360
FT /note="E->A,N: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 360
FT /note="E->Q: Reduces catalytic activity by 70%."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 426
FT /note="R->A: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24127570"
FT MUTAGEN 426
FT /note="R->K: No effect."
FT /evidence="ECO:0000269|PubMed:24127570"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:7E9S"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:3WAJ"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3WAJ"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:3WAJ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3WAJ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3WAJ"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 163..181
FT /evidence="ECO:0007829|PDB:3WAJ"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:7E9S"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:3WAJ"
FT TURN 235..238
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3WAJ"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:3WAJ"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 278..303
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:7E9S"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:7E9S"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:7E9S"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:7E9S"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3WAK"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 384..402
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 431..446
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:7E9S"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:3WAJ"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:3WAK"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3WAK"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5GMY"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:3WAJ"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 554..559
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 570..574
FT /evidence="ECO:0007829|PDB:3WAI"
FT TURN 577..580
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 584..588
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 593..602
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:3WAI"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 631..636
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 663..670
FT /evidence="ECO:0007829|PDB:3WAK"
FT HELIX 672..675
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:3WAI"
FT TURN 686..689
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 691..698
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 703..708
FT /evidence="ECO:0007829|PDB:3WAI"
FT TURN 709..711
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:5GMY"
FT HELIX 717..732
FT /evidence="ECO:0007829|PDB:3WAI"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 740..754
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 770..776
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 780..786
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 787..789
FT /evidence="ECO:0007829|PDB:3WAK"
FT STRAND 791..800
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 806..814
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 819..824
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 833..838
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 840..844
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 847..851
FT /evidence="ECO:0007829|PDB:3WAI"
FT HELIX 855..860
FT /evidence="ECO:0007829|PDB:3WAI"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:3WAI"
SQ SEQUENCE 868 AA; 98253 MW; 099D6897E559C344 CRC64;
MQNAESWFKK YWHLSVLVIA ALISVKLRIL NPWNSVFTWT VRLGGNDPWY YYRLIENTIH
NFPHRIWFDP FTYYPYGSYT HFGPFLVYLG SIAGIIFSAT SGESLRAVLA FIPAIGGVLA
ILPVYLLTRE VFDKRAAVIA AFLIAIVPGQ FLQRSILGFN DHHIWEAFWQ VSALGTFLLA
YNRWKGHDLS HNLTARQMAY PVIAGITIGL YVLSWGAGFI IAPIILAFMF FAFVLAGFVN
ADRKNLSLVA VVTFAVSALI YLPFAFNYPG FSTIFYSPFQ LLVLLGSAVI AAAFYQIEKW
NDVGFFERVG LGRKGMPLAV IVLTALIMGL FFVISPDFAR NLLSVVRVVQ PKGGALTIAE
VYPFFFTHNG EFTLTNAVLH FGALFFFGMA GILYSAYRFL KRRSFPEMAL LIWAIAMFIA
LWGQNRFAYY FAAVSAVYSA LALSVVFDKL HLYRALENAI GARNKLSYFR VAFALLIALA
AIYPTYILAD AQSSYAGGPN KQWYDALTWM RENTPDGEKY DEYYLQLYPT PQSNKEPFSY
PFETYGVISW WDYGHWIEAV AHRMPIANPF QAGIGNKYNN VPGASSFFTA ENESYAEFVA
EKLNVKYVVS DIEMETGKYY AMAVWAEGDL PLAEKYYGGY FYYSPTGTFG YANSQWDIPL
NSIIIPLRIP SELYYSTMEA KLHLFDGSGL SHYRMIYESD YPAEWKSYSS QVNLNNESQV
LQTALYEAVM RARYGVSPTM GTQEVLYKYA YTQLYEKKMG IPVKIAPSGY VKIFERVKGA
VVTGKVSANV TEVSVNATIK TNQNRTFEYW QTVEVKNGTY TVVLPYSHNS DYPVKPITPY
HIKAGNVVKE ITIYESQVQN GEIIQLDL
