SitesBLAST
Comparing BWI76_RS09045 FitnessBrowser__Koxy:BWI76_RS09045 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7kb6A Co-crystal structure of alpha glucosidase with compound 7 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 179:821/850 of 7kb6A
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(6-{[2-nitro-4-(pyrimidin-2-yl)phenyl]amino}hexyl)amino]cyclohexane-1,2,3,4-tetrol: F210 (≠ M174), W307 (≠ M274), D335 (≠ S306), I336 (≠ S307), W409 (= W382), W446 (= W417), D448 (= D419), F455 (≠ W426), R508 (= R474), D524 (= D490), F557 (= F523), H582 (= H549)
7k9tA Co-crystal structure of alpha glucosidase with compound 5 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 179:821/850 of 7k9tA
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-{[(5Z)-6-{[2-nitro-4-(2H-1,2,3-triazol-2-yl)phenyl]amino}hex-5-en-1-yl]amino}cyclohexane-1,2,3,4-tetrol: F210 (≠ M174), W307 (≠ M274), D335 (≠ S306), I336 (≠ S307), W409 (= W382), W446 (= W417), D448 (= D419), R508 (= R474), D524 (= D490), F557 (= F523), H582 (= H549)
5ieeA Murine endoplasmic reticulum alpha-glucosidase ii with 1- deoxynojirimycin (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 186:828/857 of 5ieeA
5iedA Murine endoplasmic reticulum alpha-glucosidase ii with castanospermine (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 186:828/857 of 5iedA
- binding castanospermine: W314 (≠ M274), D342 (≠ S306), I343 (≠ S307), W416 (= W382), W453 (= W417), D455 (= D419), R515 (= R474), W528 (= W487), D531 (= D490), F564 (= F523), H589 (= H549)
5h9oA Complex of murine endoplasmic reticulum alpha-glucosidase ii with d- glucose (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 186:828/857 of 5h9oA
5iefA Murine endoplasmic reticulum alpha-glucosidase ii with n-butyl-1- deoxynojirimycin (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 186:828/858 of 5iefA
- binding (2r,3r,4r,5s)-1-butyl-2-(hydroxymethyl)piperidine-3,4,5-triol: W314 (≠ M274), D342 (≠ S306), W453 (= W417), D455 (= D419), F462 (≠ W426), R515 (= R474), W528 (= W487), D531 (= D490), F564 (= F523), H589 (= H549)
7jtyA Co-crystal structure of alpha glucosidase with compound 1 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 180:822/851 of 7jtyA
- binding (1S,2S,3R,4S,5S)-5-(butylamino)-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: W308 (≠ M274), D336 (≠ S306), I337 (≠ S307), W410 (= W382), W447 (= W417), D449 (= D419), M450 (≠ N420), R509 (= R474), D525 (= D490), F558 (= F523), H583 (= H549)
7k9qA Co-crystal structure of alpha glucosidase with compound 4 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 182:824/853 of 7k9qA
- binding (1S,2S,3R,4S,5S)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: W310 (≠ M274), D338 (≠ S306), I339 (≠ S307), W449 (= W417), D451 (= D419), M452 (≠ N420), R511 (= R474), D527 (= D490), F560 (= F523), H585 (= H549)
7k9nA Co-crystal structure of alpha glucosidase with compound 2 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 182:824/853 of 7k9nA
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(9-methoxynonyl)amino]cyclohexane-1,2,3,4-tetrol: W310 (≠ M274), D338 (≠ S306), I339 (≠ S307), W412 (= W382), W449 (= W417), D451 (= D419), R511 (= R474), D527 (= D490), F560 (= F523), H585 (= H549), D589 (= D554)
7kryA Co-crystal structure of alpha glucosidase with compound 11 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 183:825/854 of 7kryA
- binding (1S,2S,3R,4S,5S)-5-({6-[(4-azido-2-nitrophenyl)amino]hexyl}amino)-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: F214 (≠ M174), W311 (≠ M274), D339 (≠ S306), I340 (≠ S307), W411 (≠ S380), C412 (≠ F381), W413 (= W382), W450 (= W417), D452 (= D419), F459 (≠ W426), D528 (= D490), F561 (= F523), H586 (= H549)
7kb8A Co-crystal structure of alpha glucosidase with compound 8 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 183:825/854 of 7kb8A
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(4-{[2-nitro-4-(triazan-1-yl)phenyl]amino}butyl)amino]cyclohexane-1,2,3,4-tetrol: F214 (≠ M174), W311 (≠ M274), D339 (≠ S306), I340 (≠ S307), W413 (= W382), W450 (= W417), D452 (= D419), F459 (≠ W426), R512 (= R474), D528 (= D490), F561 (= F523), H586 (= H549)
7kadA Co-crystal structure of alpha glucosidase with compound 6 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 183:825/854 of 7kadA
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(6-{[2-nitro-4-(1H-1,2,3-triazol-1-yl)phenyl]amino}hexyl)amino]cyclohexane-1,2,3,4-tetrol: F214 (≠ M174), W311 (≠ M274), D339 (≠ S306), I340 (≠ S307), W413 (= W382), W450 (= W417), D452 (= D419), F459 (≠ W426), D528 (= D490), F561 (= F523), H586 (= H549)
7k9oA Co-crystal structure of alpha glucosidase with compound 3 (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 183:825/854 of 7k9oA
- binding (1~{S},2~{S},3~{R},4~{S},5~{S})-1-(hydroxymethyl)-5-[6-[[2-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-4-(1,2,3,4-tetrazol-1-yl)phenyl]amino]hexylamino]cyclohexane-1,2,3,4-tetrol: F214 (≠ M174), W311 (≠ M274), D339 (≠ S306), I340 (≠ S307), W413 (= W382), W450 (= W417), D452 (= D419), M453 (≠ N420), F459 (≠ W426), R512 (= R474), D528 (= D490), F561 (= F523), H586 (= H549)
5hjrA Murine endoplasmic reticulum alpha-glucosidase ii with bound covalent intermediate (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 185:826/855 of 5hjrA
5hjoA Murine endoplasmic reticulum alpha-glucosidase ii with bound substrate analogue (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 184:825/854 of 5hjoA
- binding D-glucal: D213 (= D172), F215 (≠ M174), W413 (= W382), M453 (≠ N420), D528 (= D490)
- binding 2-deoxy-alpha-D-arabino-hexopyranose: W311 (≠ M274), D339 (≠ S306), I340 (≠ S307), W450 (= W417), D452 (= D419), R512 (= R474), D528 (= D490), F561 (= F523), H586 (= H549)
5iegA Murine endoplasmic reticulum alpha-glucosidase ii with n-9'- methoxynonyl-1-deoxynojirimycin (see paper)
31% identity, 81% coverage: 147:787/787 of query aligns to 186:825/856 of 5iegA
- binding N-9'-methoxynonyl-1-deoxynojirimycin: F217 (≠ M174), W314 (≠ M274), D342 (≠ S306), I343 (≠ S307), W450 (= W417), D452 (= D419), R512 (= R474), W525 (= W487), D528 (= D490), F561 (= F523), H586 (= H549)
Q14697 Neutral alpha-glucosidase AB; Alpha-glucosidase 2; Glucosidase II subunit alpha; EC 3.2.1.207 from Homo sapiens (Human) (see 6 papers)
30% identity, 81% coverage: 147:787/787 of query aligns to 254:915/944 of Q14697
- R309 (≠ V198) to C: no effect on PKD1 and PKD2 localization to the cell surface; dbSNP:rs1063445
- T383 (= T256) to R: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs879255642
- R400 (≠ T273) to L: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs770519542
- D542 (= D419) mutation to N: Loss of activity.
- R590 (= R462) to P: found in a patient with polycystic liver disease; uncertain significance; dbSNP:rs1465649718
- H785 (≠ Y658) to N: found in a patient affected by polycystic liver disease; uncertain significance; the patient carried additional PKHD1 variant; the mutation results in significantly reduced alpha-glucosidase activity; dbNP:rs753910059; dbSNP:rs753910059
- R817 (= R690) to W: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs879255643
- H850 (≠ E723) to Y: in dbSNP:rs114915323
Sites not aligning to the query:
- 4:5 natural variant: Missing (in PKD3; uncertain significance; no apparent effect on the endoplasmic reticulum localization; dbSNP:rs750723025)
- 95 Q → R: no effect on PKD1 and PKD2 localization to the cell surface; dbSNP:rs1392032530
- 97 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 232 T → A: no effect on PKD1 and PKD2 localization to the cell surface
- 815:944 natural variant: Missing (found in a patient with polycystic liver disease; uncertain significance; no apparent effect on the endoplasmic reticulum localization)
- 864:944 natural variant: Missing (found in a patient with polycystic liver disease; uncertain significance; no apparent effect on the endoplasmic reticulum localization; dbSNP:rs1210158408)
- 918:944 natural variant: Missing (found in a patient affected by polycystic liver disease; uncertain significance)
Q8BHN3 Neutral alpha-glucosidase AB; Alpha-glucosidase 2; Glucosidase II subunit alpha; EC 3.2.1.207 from Mus musculus (Mouse) (see 3 papers)
31% identity, 81% coverage: 147:787/787 of query aligns to 254:915/944 of Q8BHN3
- D542 (= D419) active site, Nucleophile; mutation D->E,N: Loss of enzyme activity.
- D618 (= D490) active site, Proton donor; mutation to N: Loss of enzyme activity.
- C633 (≠ G505) modified: Disulfide link with 644
- C644 (≠ V516) modified: Disulfide link with 633
- R818 (≠ H691) mutation to E: Disrupts interaction with PRKCSH. Nearly abolishes enzyme activity.
Sites not aligning to the query:
- 1:32 signal peptide
- 41 modified: Disulfide link with 47
- 47 modified: Disulfide link with 41
- 97 modified: carbohydrate, N-linked (GlcNAc...) asparagine
6jr7A Flavobacterium johnsoniae gh31 dextranase, fjdex31a, complexed with glucose (see paper)
31% identity, 82% coverage: 81:728/787 of query aligns to 69:707/812 of 6jr7A
- binding alpha-D-glucopyranose: G249 (≠ M274), D277 (≠ S306), W352 (= W382), W352 (= W382), W386 (= W417), D388 (= D419), R445 (= R474), D461 (= D490), Y500 (≠ F523), H530 (= H549), G533 (≠ D554)
Q9FN05 Probable glucan 1,3-alpha-glucosidase; Glucosidase II subunit alpha; Protein PRIORITY IN SWEET LIFE 5; Protein RADIAL SWELLING 3; EC 3.2.1.84 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 74% coverage: 150:733/787 of query aligns to 236:829/921 of Q9FN05
- S517 (≠ E424) mutation to F: In psl5-1; Compromised defense response induced by the bacterial elicitor elongation factor Tu (EF-Tu).
- S599 (≠ N501) mutation to F: In rsw3; temperature-sensitive radial swelling of roots and reduction in cellulose production.
Query Sequence
>BWI76_RS09045 FitnessBrowser__Koxy:BWI76_RS09045
MKTLKNWTLHQRLEHHVELLVDGQHTLCLYVLEENMFRVLLKRHGQLALDRTWSIAPGQD
VPWEGRPREELSGFSLPAWQLTEHSDALTIATDQLRVTVHQPLWLEWRYRDEAGEWQPLA
NDRPTSAYLANAHGDGVAHYLSRRKDERFYGLGEKAGDLQRNGKRYEMRNLDAMGYNAAS
TDPLYKHIPFTITQRSDVSYGLFYDNLSSCWLDLGNEIDNYHTAYRRWQAEAGDIDYYLF
SGKRVLDITKAFVRLTGKTLFGPKWSLGYSGSTMHYTDAPDAQNQLMNFIRLCDEHAIPC
DSFQLSSGYTSINGKRYVFNWNNDKVPQPKVMSQAFHDAGLKLAANIKPCLLQDHPRYHE
VAERGLFIRDSQADAPERSSFWDDEGSHLDFTNPQTVAWWQEGVTTQLLELGIDSTWNDN
NEYEVWDGEARCHGFGHEIAIKHIRPVMPLLMMRASLEAQQRFAPQKRPYLISRSGCAGM
QRYVQTWSGDNRTNWETLRYNTRMGLGMSLSGLFNVGHDVGGFSGDKPDPELFVRWVQNG
VMHPRFTIHSWNDDQTVNEAWMYPEVTPAIRSAIELRYRLLPYLYTLLWQAHADDEPMLR
PTFLDHEHDAQTFAECDDFLLGRDLLVASVVEPGARQRRVWLPANQDGWYDFYSHQWYAG
GQWIVLDAPLEKLPLLVRAGAGLPLSERIRHVCAEKDDTRELKLFPLKGMGTCRGLLFED
DGESWGYRNGNALWVEWEMVCDSASINLKVKARGDYRPAWKALKVSLPAGEKRRLRVNGE
KRSEWRV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory