SitesBLAST
Comparing Echvi_2842 FitnessBrowser__Cola:Echvi_2842 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6jr7A Flavobacterium johnsoniae gh31 dextranase, fjdex31a, complexed with glucose (see paper)
34% identity, 86% coverage: 42:732/808 of query aligns to 31:734/812 of 6jr7A
- binding alpha-D-glucopyranose: G249 (≠ Y259), D277 (= D287), W352 (vs. gap), W352 (vs. gap), W386 (= W395), D388 (= D397), R445 (= R455), D461 (= D471), Y500 (≠ F504), H530 (= H529), G533 (≠ N533)
7kb6A Co-crystal structure of alpha glucosidase with compound 7 (see paper)
32% identity, 80% coverage: 62:705/808 of query aligns to 113:761/850 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 (= F164), W307 (≠ Y259), D335 (= D287), I336 (= I288), W409 (= W361), W446 (= W395), D448 (= D397), F455 (≠ W404), R508 (= R455), D524 (= D471), F557 (= F504), H582 (= H529)
7k9tA Co-crystal structure of alpha glucosidase with compound 5 (see paper)
32% identity, 80% coverage: 62:705/808 of query aligns to 113:761/850 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 (= F164), W307 (≠ Y259), D335 (= D287), I336 (= I288), W409 (= W361), W446 (= W395), D448 (= D397), R508 (= R455), D524 (= D471), F557 (= F504), H582 (= H529)
5hjoA Murine endoplasmic reticulum alpha-glucosidase ii with bound substrate analogue (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 200:765/854 of 5hjoA
- binding D-glucal: D213 (= D162), F215 (= F164), W413 (= W361), M453 (= M398), D528 (= D471)
- binding 2-deoxy-alpha-D-arabino-hexopyranose: W311 (≠ Y259), D339 (= D287), I340 (= I288), W450 (= W395), D452 (= D397), R512 (= R455), D528 (= D471), F561 (= F504), H586 (= H529)
5hjrA Murine endoplasmic reticulum alpha-glucosidase ii with bound covalent intermediate (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 201:766/855 of 5hjrA
Q14697 Neutral alpha-glucosidase AB; Alpha-glucosidase 2; Glucosidase II subunit alpha; EC 3.2.1.207 from Homo sapiens (Human) (see 6 papers)
34% identity, 69% coverage: 149:705/808 of query aligns to 270:855/944 of Q14697
- R309 (≠ L187) to C: no effect on PKD1 and PKD2 localization to the cell surface; dbSNP:rs1063445
- T383 (= T241) to R: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs879255642
- R400 (= R258) to L: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs770519542
- D542 (= D397) mutation to N: Loss of activity.
- R590 (≠ S443) to P: found in a patient with polycystic liver disease; uncertain significance; dbSNP:rs1465649718
- H785 (≠ Y637) 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 (≠ S669) to W: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs879255643
- H850 (≠ V700) 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)
5iefA Murine endoplasmic reticulum alpha-glucosidase ii with n-butyl-1- deoxynojirimycin (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 202:768/858 of 5iefA
- binding (2r,3r,4r,5s)-1-butyl-2-(hydroxymethyl)piperidine-3,4,5-triol: W314 (≠ Y259), D342 (= D287), W453 (= W395), D455 (= D397), F462 (≠ W404), R515 (= R455), W528 (= W468), D531 (= D471), F564 (= F504), H589 (= H529)
5ieeA Murine endoplasmic reticulum alpha-glucosidase ii with 1- deoxynojirimycin (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 202:768/857 of 5ieeA
5iedA Murine endoplasmic reticulum alpha-glucosidase ii with castanospermine (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 202:768/857 of 5iedA
- binding castanospermine: W314 (≠ Y259), D342 (= D287), I343 (= I288), W416 (= W361), W453 (= W395), D455 (= D397), R515 (= R455), W528 (= W468), D531 (= D471), F564 (= F504), H589 (= H529)
5h9oA Complex of murine endoplasmic reticulum alpha-glucosidase ii with d- glucose (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 202:768/857 of 5h9oA
7jtyA Co-crystal structure of alpha glucosidase with compound 1 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 196:762/851 of 7jtyA
- binding (1S,2S,3R,4S,5S)-5-(butylamino)-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: W308 (≠ Y259), D336 (= D287), I337 (= I288), W410 (= W361), W447 (= W395), D449 (= D397), M450 (= M398), R509 (= R455), D525 (= D471), F558 (= F504), H583 (= H529)
7kryA Co-crystal structure of alpha glucosidase with compound 11 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 199:765/854 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 (= F164), W311 (≠ Y259), D339 (= D287), I340 (= I288), W411 (≠ Q359), C412 (≠ V360), W413 (= W361), W450 (= W395), D452 (= D397), F459 (≠ W404), D528 (= D471), F561 (= F504), H586 (= H529)
7kb8A Co-crystal structure of alpha glucosidase with compound 8 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 199:765/854 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 (= F164), W311 (≠ Y259), D339 (= D287), I340 (= I288), W413 (= W361), W450 (= W395), D452 (= D397), F459 (≠ W404), R512 (= R455), D528 (= D471), F561 (= F504), H586 (= H529)
7kadA Co-crystal structure of alpha glucosidase with compound 6 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 199:765/854 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 (= F164), W311 (≠ Y259), D339 (= D287), I340 (= I288), W413 (= W361), W450 (= W395), D452 (= D397), F459 (≠ W404), D528 (= D471), F561 (= F504), H586 (= H529)
7k9oA Co-crystal structure of alpha glucosidase with compound 3 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 199:765/854 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 (= F164), W311 (≠ Y259), D339 (= D287), I340 (= I288), W413 (= W361), W450 (= W395), D452 (= D397), M453 (= M398), F459 (≠ W404), R512 (= R455), D528 (= D471), F561 (= F504), H586 (= H529)
7k9qA Co-crystal structure of alpha glucosidase with compound 4 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 198:764/853 of 7k9qA
- binding (1S,2S,3R,4S,5S)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: W310 (≠ Y259), D338 (= D287), I339 (= I288), W449 (= W395), D451 (= D397), M452 (= M398), R511 (= R455), D527 (= D471), F560 (= F504), H585 (= H529)
7k9nA Co-crystal structure of alpha glucosidase with compound 2 (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 198:764/853 of 7k9nA
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(9-methoxynonyl)amino]cyclohexane-1,2,3,4-tetrol: W310 (≠ Y259), D338 (= D287), I339 (= I288), W412 (= W361), W449 (= W395), D451 (= D397), R511 (= R455), D527 (= D471), F560 (= F504), H585 (= H529), D589 (≠ N533)
Q8BHN3 Neutral alpha-glucosidase AB; Alpha-glucosidase 2; Glucosidase II subunit alpha; EC 3.2.1.207 from Mus musculus (Mouse) (see 3 papers)
33% identity, 69% coverage: 149:705/808 of query aligns to 270:855/944 of Q8BHN3
- D542 (= D397) active site, Nucleophile; mutation D->E,N: Loss of enzyme activity.
- D618 (= D471) active site, Proton donor; mutation to N: Loss of enzyme activity.
- C633 (≠ V486) modified: Disulfide link with 644
- C644 (≠ A497) modified: Disulfide link with 633
- R818 (≠ H670) 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
5iegA Murine endoplasmic reticulum alpha-glucosidase ii with n-9'- methoxynonyl-1-deoxynojirimycin (see paper)
34% identity, 69% coverage: 149:705/808 of query aligns to 202:765/856 of 5iegA
- binding N-9'-methoxynonyl-1-deoxynojirimycin: F217 (= F164), W314 (≠ Y259), D342 (= D287), I343 (= I288), W450 (= W395), D452 (= D397), R512 (= R455), W525 (= W468), D528 (= D471), F561 (= F504), H586 (= H529)
7kbrA Co-crystal structure of alpha glucosidase with compound 10 (see paper)
36% identity, 61% coverage: 215:705/808 of query aligns to 10:508/597 of 7kbrA
- binding 2-{[2-nitro-4-(triazan-1-yl)phenyl]amino}ethyl (2-{[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexyl]amino}ethyl)carbamate: W54 (≠ Y259), D82 (= D287), I83 (= I288), P96 (≠ G301), T97 (≠ E302), P100 (= P305), W154 (≠ Q359), C155 (≠ V360), W156 (= W361), W193 (= W395), D195 (= D397), M196 (= M398), F202 (≠ W404), R255 (= R455), D271 (= D471), F304 (= F504), H329 (= H529), H331 (≠ M531)
Query Sequence
>Echvi_2842 FitnessBrowser__Cola:Echvi_2842
MTTVATSVNRAQNQSAGKVMSWEQTPHGIAGITDKAYFNICLYTAKIVRVQVSRTVPFTP
NPYSVVASPEETPVNLHEEADFLILETKDLKIVLNKNEWALTYYDQNGNLLNQDDPAFGV
SWLGTEVTNYKKLQPHEKFIGLGEKTGGIDRAGQAFVNWNTDYFAYGVNDDPLYMSIPFY
IGIHQELAYGIFFDNTHKTTFNFGASNRRFSYFSADDGDMDYYFFQGDSVSEIIGGYTSL
TGKLALPPKWALGFQQCRYSYYPESEVFTLAKTFRDKDMPADVIYLDIHHMKKYKVFTFD
GEKFPNPKAMIKALNAKGFRVVVIMDPGIKVEKDYLPYEEGMDQDLFLKYPDGETYEGQV
WPGWCAFPDFTAAKTREWWAEKMAFYTDAGVDGFWTDMNEPASWGQHTPNLINFDYEGEQ
VSHRKARNIYGMQMARAAQNGASTNGQERPFILTRAGFSGIQRFAAAWTGDNVASEEHML
AGIRLVNSLGISGVSFAGYDVGGFCGEASKSLFARWMSIAAFAPLYRAHSMINSNDAEPW
AFGEEVEEISKNYLKLRYKMLPLWYSAFYKSTQDGLPVAKSLAIDYCFDDHVYDARFQNQ
YICCDALLVVPVESHKEITKAYLPEGQWYYLYNDDSYKGAQEIYVDTPINYLPVFVKGGS
ILPLQSPVSHTAEQHDGILRLHVYKGEGTSSYIHYEDDGVTLDYQKGKHHKRTITLDSDQ
QELVLSTVEGDFTSSFTALQVYFHGFSVGTATINGNQASVHREQLAFLQPITDFDPLPDN
RLPYYEIEEIPVVTVPYDRDKITVIFDQ
Or try a new SitesBLAST search
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