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GH101_STRR6
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   03-AUG-2022, entry version 124.
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; Firmicutes; 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   EnsemblBacteria; AAK99132; AAK99132; spr0328.
DR   GeneID; 60232804; -.
DR   KEGG; spr:spr0328; -.
DR   PATRIC; fig|171101.6.peg.367; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_001105_0_0_9; -.
DR   OMA; NPQGWEK; -.
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; 2.60.40.1180; -; 1.
DR   Gene3D; 2.70.98.10; -; 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; IPR040502; GalBD-like.
DR   InterPro; IPR014718; GH-type_carb-bd.
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; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF18080; Gal_mutarotas_3; 1.
DR   Pfam; PF17974; GalBD_like; 1.
DR   Pfam; PF17995; GH101_N; 1.
DR   Pfam; PF17451; Glyco_hyd_101C; 1.
DR   Pfam; PF12905; Glyco_hydro_101; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 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
 
 
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