ID GH101_STRR6 Reviewed; 1767 AA.
AC Q8DR60;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Endo-alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.97 {ECO:0000269|PubMed:21877};
DE AltName: Full=SpGH101;
DE Flags: Precursor;
GN OrderedLocusNames=spr0328;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PH DEPENDENCE.
RX PubMed=21877; DOI=10.1016/s0021-9258(19)75264-8;
RA Umemoto J., Bhavanandan V.P., Davidson E.A.;
RT "Purification and properties of an endo-alpha-N-acetyl-D-galactosaminidase
RT from Diplococcus pneumoniae.";
RL J. Biol. Chem. 252:8609-8614(1977).
RN [3]
RP FUNCTION, O-GLYCANASE ACTIVITY, KINETIC PARAMETERS, REACTION MECHANISM,
RP ACTIVE SITES, GLYCAN-BINDING STUDIES, AND MUTAGENESIS OF ASP-658; ASP-764
RP AND GLU-796.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=19788271; DOI=10.1021/bi9013825;
RA Willis L.M., Zhang R., Reid A., Withers S.G., Wakarchuk W.W.;
RT "Mechanistic investigation of the endo-alpha-N-acetylgalactosaminidase from
RT Streptococcus pneumoniae R6.";
RL Biochemistry 48:10334-10341(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 40-1567 IN COMPLEX WITH CALCIUM,
RP FUNCTION, AND DOMAIN.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=18784084; DOI=10.1074/jbc.c800150200;
RA Caines M.E., Zhu H., Vuckovic M., Willis L.M., Withers S.G.,
RA Wakarchuk W.W., Strynadka N.C.;
RT "The structural basis for T-antigen hydrolysis by Streptococcus pneumoniae:
RT a target for structure-based vaccine design.";
RL J. Biol. Chem. 283:31279-31283(2008).
CC -!- FUNCTION: Involved in the breakdown of mucin-type O-linked glycans.
CC Specifically removes the T-antigen disaccharide (Gal-beta-1,3-GalNAc-
CC alpha) from extracellular host glycoproteins. Representative of a
CC broadly important class of virulence factors.
CC {ECO:0000269|PubMed:18784084, ECO:0000269|PubMed:19788271,
CC ECO:0000269|PubMed:21877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-threonyl-[protein] = beta-D-galactosyl-(1->3)-N-
CC acetyl-D-galactosamine + L-threonyl-[protein]; Xref=Rhea:RHEA:54540,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13923, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:137950, ChEBI:CHEBI:546807;
CC EC=3.2.1.97; Evidence={ECO:0000269|PubMed:21877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-seryl-[protein] = beta-D-galactosyl-(1->3)-N-
CC acetyl-D-galactosamine + L-seryl-[protein]; Xref=Rhea:RHEA:30983,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13922, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:137949, ChEBI:CHEBI:546807;
CC EC=3.2.1.97; Evidence={ECO:0000269|PubMed:21877};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for Gal-beta-1,3-GalNAc-alpha-2,4-dinitrophenyl
CC {ECO:0000269|PubMed:19788271};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:21877};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- DOMAIN: Is a multimodular protein that comprises seven distinct
CC domains. The catalytic glycoside hydrolase domain resides in domain 3
CC (residues 602-893). Possesses four potential carbohydrate-binding
CC modules (CBMs). {ECO:0000269|PubMed:18784084}.
CC -!- MISCELLANEOUS: The hydrolysis reaction catalyzed by SpGH101 proceeds
CC with retention of the anomeric configuration.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 101 family. A subfamily.
CC {ECO:0000305}.
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DR EMBL; AE007317; AAK99132.1; -; Genomic_DNA.
DR PIR; H97912; H97912.
DR RefSeq; NP_357922.1; NC_003098.1.
DR RefSeq; WP_001032523.1; NC_003098.1.
DR PDB; 3ECQ; X-ray; 2.90 A; A/B=40-1567.
DR PDBsum; 3ECQ; -.
DR AlphaFoldDB; Q8DR60; -.
DR SMR; Q8DR60; -.
DR STRING; 171101.spr0328; -.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR CAZy; GH101; Glycoside Hydrolase Family 101.
DR KEGG; spr:spr0328; -.
DR PATRIC; fig|171101.6.peg.367; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_001105_0_0_9; -.
DR BRENDA; 3.2.1.97; 11933.
DR EvolutionaryTrace; Q8DR60; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050110; F:mucinaminylserine mucinaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd14244; GH_101_like; 1.
DR Gene3D; 2.60.120.870; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 6.10.140.660; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR025706; Endoa_GalNAc.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR040633; Gal_mutarotas_3.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR049314; GH101_dom-5.
DR InterPro; IPR040502; GH101_dom-6.
DR InterPro; IPR040575; GH101_N.
DR InterPro; IPR035364; Glyco_hyd_101_beta.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR048842; SpGH101_helical.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; NF040533; endo_SpGH101; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF18080; Gal_mutarotas_3; 1.
DR Pfam; PF17974; GalBD_like; 1.
DR Pfam; PF21466; GH101_dom-5; 1.
DR Pfam; PF17995; GH101_N; 1.
DR Pfam; PF17451; Glyco_hyd_101C; 1.
DR Pfam; PF12905; Glyco_hydro_101; 1.
DR Pfam; PF20909; SpGH101_helical; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell wall; Glycosidase; Hydrolase; Metal-binding;
KW Peptidoglycan-anchor; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..1738
FT /note="Endo-alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000408870"
FT PROPEP 1739..1767
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000408871"
FT REGION 63..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..893
FT /note="Catalytic"
FT MOTIF 1735..1739
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 82..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 764
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19788271"
FT ACT_SITE 796
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:19788271"
FT BINDING 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 583
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 588
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 658
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 1233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 1235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 1281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 1284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18784084"
FT BINDING 1411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18784084"
FT MOD_RES 1738
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT MUTAGEN 658
FT /note="D->A: Large decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:19788271"
FT MUTAGEN 764
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19788271"
FT MUTAGEN 796
FT /note="E->A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19788271"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 337..348
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 390..399
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 404..415
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 418..430
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 494..503
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 529..537
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 569..576
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 586..593
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 594..596
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 603..608
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 609..616
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 626..640
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 644..650
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 673..685
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 689..700
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 709..711
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 722..733
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 735..740
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 743..754
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 760..765
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 776..787
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 792..796
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 802..804
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 806..808
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 809..812
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 814..817
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 827..833
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 834..836
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 845..847
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 849..851
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 867..869
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 874..890
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 893..900
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 904..908
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 911..915
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 918..924
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 930..936
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 943..946
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 948..952
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 955..959
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 962..967
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 978..980
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 982..989
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 991..996
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 999..1002
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1007..1012
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1015..1021
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1026..1032
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1039..1044
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 1053..1058
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1072..1076
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1078..1080
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1081..1085
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1091..1095
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1097..1100
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1102..1107
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1116..1125
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1127..1129
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1131..1136
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1141..1148
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1164..1166
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1176..1183
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1192..1197
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1199..1202
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1204..1213
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1219..1221
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1223..1225
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1230..1232
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 1240..1243
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1244..1246
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1251..1254
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1256..1261
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 1264..1267
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1271..1273
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1284..1290
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1296..1301
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 1303..1305
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1313..1324
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1327..1336
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1339..1341
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1346..1348
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1349..1353
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1365..1372
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1379..1385
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1397..1403
FT /evidence="ECO:0007829|PDB:3ECQ"
FT TURN 1404..1406
FT /evidence="ECO:0007829|PDB:3ECQ"
FT STRAND 1407..1418
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1422..1437
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1444..1450
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1452..1458
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1466..1475
FT /evidence="ECO:0007829|PDB:3ECQ"
FT HELIX 1477..1480
FT /evidence="ECO:0007829|PDB:3ECQ"
SQ SEQUENCE 1767 AA; 196144 MW; 34231975797B7587 CRC64;
MNKGLFEKRC KYSIRKFSLG VASVMIGATF FGTSPVLADS VQSGSTANLP ADLATALATA
KENDGHDFEA PKVGEDQGSP EVTDGPKTEE ELLALEKEKP AEEKPKEDKP AAAKPETPKT
VTPEWQTVEK KEQQGTVTIR EEKGVRYNQL SSTAQNDNAG KPALFEKKGL TVDANGNATV
DLTFKDDSEK GKSRFGVFLK FKDTKNNVFV GYDKDGWFWE YKSPTTSTWY RGSRVAAPET
GSTNRLSITL KSDGQLNASN NDVNLFDTVT LPAAVNDHLK NEKKILLKAG SYDDERTVVS
VKTDNQEGVK TEDTPAEKET GPEVDDSKVT YDTIQSKVLK AVIDQAFPRV KEYSLNGHTL
PGQVQQFNQV FINNHRITPE VTYKKINETT AEYLMKLRDD AHLINAEMTV RLQVVDNQLH
FDVTKIVNHN QVTPGQKIDD ERKLLSSISF LGNALVSVSS DQTGAKFDGA TMSNNTHVSG
DDHIDVTNPM KDLAKGYMYG FVSTDKLAAG VWSNSQNSYG GGSNDWTRLT AYKETVGNAN
YVGIHSSEWQ WEKAYKGIVF PEYTKELPSA KVVITEDANA DKKVDWQDGA IAYRSIMNNP
QGWKKVKDIT AYRIAMNFGS QAQNPFLMTL DGIKKINLHT DGLGQGVLLK GYGSEGHDSG
HLNYADIGKR IGGVEDFKTL IEKAKKYGAH LGIHVNASET YPESKYFNEK ILRKNPDGSY
SYGWNWLDQG INIDAAYDLA HGRLARWEDL KKKLGDGLDF IYVDVWGNGQ SGDNGAWATH
VLAKEINKQG WRFAIEWGHG GEYDSTFHHW AADLTYGGYT NKGINSAITR FIRNHQKDAW
VGDYRSYGGA ANYPLLGGYS MKDFEGWQGR SDYNGYVTNL FAHDVMTKYF QHFTVSKWEN
GTPVTMTDNG STYKWTPEMR VELVDADNNK VVVTRKSNDV NSPQYRERTV TLNGRVIQDG
SAYLTPWNWD ANGKKLSTDK EKMYYFNTQA GATTWTLPSD WAKSKVYLYK LTDQGKTEEQ
ELTVKDGKIT LDLLANQPYV LYRSKQTNPE MSWSEGMHIY DQGFNSGTLK HWTISGDASK
AEIVKSQGAN DMLRIQGNKE KVSLTQKLTG LKPNTKYAVY VGVDNRSNAK ASITVNTGEK
EVTTYTNKSL ALNYVKAYAH NTRRNNATVD DTSYFQNMYA FFTTGSDVSN VTLTLSREAG
DEATYFDEIR TFENNSSMYG DKHDTGKGTF KQDFENVAQG IFPFVVGGVE GVEDNRTHLS
EKHDPYTQRG WNGKKVDDVI EGNWSLKTNG LVSRRNLVYQ TIPQNFRFEA GKTYRVTFEY
EAGSDNTYAF VVGKGEFQSG RRGTQASNLE MHELPNTWTD SKKAKKATFL VTGAETGDTW
VGIYSTGNAS NTRGDSGGNA NFRGYNDFMM DNLQIEEITL TGKMLTENAL KNYLPTVAMT
NYTKESMDAL KEAVFNLSQA DDDISVEEAR AEIAKIEALK NALVQKKTAL VADDFASLTA
PAQAQEGLAN AFDGNLSSLW HTSWGGGDVG KPATMVLKEA TEITGLRYVP RGSGSNGNLR
DVKLVVTDES GKEHTFTATD WPDNNKPKDI DFGKTIKAKK IVLTGTKTYG DGGDKYQSAA
ELIFTRPQVA ETPLDLSGYE AALAKAQKLT DKDNQEEVAS VQASMKYATD NHLLTERMVE
YFADYLNQLK DSATKPDAPT VEKPEFKLSS VASDQGKTPD YKQEIARPET PEQILPATGE
SQFDTALFLA SVSLALSALF VVKTKKD
//
