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GH101_STRPN
ID   GH101_STRPN             Reviewed;        1767 AA.
AC   Q2MGH6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Endo-alpha-N-acetylgalactosaminidase;
DE            EC=3.2.1.97 {ECO:0000250|UniProtKB:Q8DR60};
DE   AltName: Full=SpGH101;
DE   Flags: Precursor;
GN   OrderedLocusNames=SP_0368;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   BIOTECHNOLOGY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=18166586; DOI=10.1084/jem.20071168;
RA   Giefing C., Meinke A.L., Hanner M., Henics T., Bui M.D., Gelbmann D.,
RA   Lundberg U., Senn B.M., Schunn M., Habel A., Henriques-Normark B.,
RA   Ortqvist A., Kalin M., von Gabain A., Nagy E.;
RT   "Discovery of a novel class of highly conserved vaccine antigens using
RT   genomic scale antigenic fingerprinting of pneumococcus with human
RT   antibodies.";
RL   J. Exp. Med. 205:117-131(2008).
RN   [3]
RP   FAMILY ASSIGNMENT.
RX   PubMed=20556855; DOI=10.1142/s0219720010004628;
RA   Naumoff D.G.;
RT   "GH101 family of glycoside hydrolases: subfamily structure and evolutionary
RT   connections with other families.";
RL   J. Bioinform. Comput. Biol. 8:437-451(2010).
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:0000250|UniProtKB:Q8DR60}.
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:0000250|UniProtKB:Q8DR60};
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:0000250|UniProtKB:Q8DR60};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000305|PubMed:18166586}; Peptidoglycan-anchor
CC       {ECO:0000305|PubMed:18166586}. Note=Has been shown to be localized at
CC       the cell surface.
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) (By similarity). {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: Was identified as a vaccine antigen as it provides
CC       significant cross-protection in a stringent mouse model of lethal
CC       sepsis. {ECO:0000269|PubMed:18166586}.
CC   -!- MISCELLANEOUS: The hydrolysis reaction catalyzed by SpGH101 proceeds
CC       with retention of the anomeric configuration. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 101 family. A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005672; ABC75807.1; -; Genomic_DNA.
DR   RefSeq; WP_001032461.1; NZ_AKVY01000001.1.
DR   PDB; 5A55; X-ray; 1.85 A; A=317-1425.
DR   PDB; 5A56; X-ray; 1.80 A; A=317-1425.
DR   PDB; 5A57; X-ray; 1.46 A; A=317-1426.
DR   PDB; 5A58; X-ray; 1.80 A; A=317-1426.
DR   PDB; 5A59; X-ray; 2.50 A; A=317-1426.
DR   PDB; 5A5A; X-ray; 1.75 A; A=317-1426.
DR   PDBsum; 5A55; -.
DR   PDBsum; 5A56; -.
DR   PDBsum; 5A57; -.
DR   PDBsum; 5A58; -.
DR   PDBsum; 5A59; -.
DR   PDBsum; 5A5A; -.
DR   AlphaFoldDB; Q2MGH6; -.
DR   SMR; Q2MGH6; -.
DR   STRING; 170187.SP_0368; -.
DR   CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR   CAZy; GH101; Glycoside Hydrolase Family 101.
DR   EnsemblBacteria; ABC75807; ABC75807; SP_0368.
DR   KEGG; spn:SP_0368; -.
DR   eggNOG; COG0366; Bacteria.
DR   OMA; NPQGWEK; -.
DR   PhylomeDB; Q2MGH6; -.
DR   BioCyc; SPNE170187:G1FZB-379-MON; -.
DR   Proteomes; UP000000585; 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; Secreted; Signal; Virulence.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..1738
FT                   /note="Endo-alpha-N-acetylgalactosaminidase"
FT                   /id="PRO_0000408868"
FT   PROPEP          1739..1767
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000408869"
FT   REGION          61..124
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                   /evidence="ECO:0000250"
FT   REGION          1711..1730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250"
FT   ACT_SITE        796
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         577
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         579
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         581
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         583
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         588
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         658
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1235
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1411
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1738
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          337..344
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          350..355
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          358..361
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          370..372
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          375..377
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          380..387
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          390..399
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           400..402
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          404..415
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          418..428
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           441..443
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          447..449
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          455..459
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          466..470
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          481..485
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          494..503
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          508..513
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          519..521
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           522..524
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          529..536
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          539..546
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           562..564
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          569..576
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          578..582
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           586..593
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            594..596
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           603..608
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          609..616
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           626..639
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          644..650
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            669..672
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           673..684
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           685..687
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          689..700
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           709..711
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          722..733
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           735..740
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           743..754
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          760..765
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           776..788
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          792..797
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            802..804
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          806..808
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           809..812
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          821..823
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           827..833
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           834..836
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           845..847
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           849..851
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          864..866
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           867..869
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           873..890
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          893..900
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          904..908
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          911..915
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          918..924
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          930..936
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           943..946
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          948..952
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          955..959
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          962..967
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           978..980
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          982..989
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          993..996
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           999..1002
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1007..1012
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1015..1021
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1028..1031
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1039..1044
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            1053..1058
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1072..1076
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           1078..1080
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1081..1085
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1091..1095
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1097..1100
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1102..1107
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1116..1125
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1127..1129
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1131..1136
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1141..1148
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           1164..1166
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1176..1183
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1192..1197
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1199..1202
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1204..1213
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1222..1225
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1230..1232
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            1240..1243
FT                   /evidence="ECO:0007829|PDB:5A5A"
FT   STRAND          1244..1246
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1251..1254
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1256..1261
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            1264..1267
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           1271..1273
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1284..1288
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1296..1301
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            1303..1305
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1313..1324
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1327..1336
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1350..1353
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1357..1360
FT                   /evidence="ECO:0007829|PDB:5A5A"
FT   STRAND          1365..1373
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1379..1385
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           1397..1403
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   TURN            1404..1406
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   STRAND          1408..1418
FT                   /evidence="ECO:0007829|PDB:5A57"
FT   HELIX           1422..1426
FT                   /evidence="ECO:0007829|PDB:5A57"
SQ   SEQUENCE   1767 AA;  196060 MW;  2F48378BBD53FA1D CRC64;
     MNKGLFEKRC KYSIRKFSLG VASVMIGAAF FGTSPVLADS VQSGSTANLP ADLATALATA
     KENDGRDFEA PKVGEDQGSP EVTDGPKTEE ELLALEKEKP AEEKPKEDKP AAAKPETPKT
     VTPEWQTVAN 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 ESKLLSSISF LGNALVSVSS NQTGAKFDGA TMSNNTHVSG
     DDHIDVTNPM KDLAKGYMYG FVSTDKLAAG VWSNSQNSYG GGSNDWTRLT AYKETVGNAN
     YVGIHSSEWQ WEKAYKGIVF PEYTKELPSA KVVITEDANA DKNVDWQDGA IAYRSIMNNP
     QGWEKVKDIT 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 NTRRDNATVD DTSYFQNMYA FFTTGADVSN VTLTLSREAG
     DQATYFDEIR TFENNSSMYG DKHDTGKGTF KQDFENVAQG IFPFVVGGVE GVEDNRTHLS
     EKHNPYTQRG WNGKKVDDVI EGNWSLKTNG LVSRRNLVYQ TIPQNFRFEA GKTYRVTFEY
     EAGSDNTYAF VVGKGEFQSG RRGTQASNLE MHELPNTWTD SKKAKKATFL VTGAETGDTW
     VGIYSTGNAS NTRGDSGGNA NFRGYNDFMM DNLQIEEITL TGKMLTENAL KNYLPTVAMT
     NYTKESMDAL KEAVFNLSQA DDDISVEEAR AEIAKIEALK NALVQKKTAL VADDFASLTA
     PAQAQEGLAN AFDGNVSSLW HTSWNGGDVG KPATMVLKEP TEITGLRYVP RGSGSNGNLR
     DVKLVVTDES GKEHTFTATD WPNNNKPKDI DFGKTIKAKK IVLTGTKTYG DGGDKYQSAA
     ELIFTRPQVA ETPLDLSGYE AALVKAQKLT DKDNQEEVAS VQASMKYATD NHLLTERMVE
     YFADYLNQLK DSATKPDAPT VEKPEFKLRS LASEQGKTPD YKQEIARPET PEQILPATGE
     SQSDTALILA SVSLALSALF VVKTKKD
 
 
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