SitesBLAST
Comparing HSERO_RS20525 FitnessBrowser__HerbieS:HSERO_RS20525 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)
26% identity, 93% coverage: 13:757/803 of query aligns to 11:733/812 of 6jr7A
- binding alpha-D-glucopyranose: G249 (≠ M280), D277 (≠ S312), W352 (≠ E389), W352 (≠ E389), W386 (= W422), D388 (= D424), R445 (= R479), D461 (= D495), Y500 (≠ F528), H530 (= H554), G533 (≠ D559)
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, 72% coverage: 153:733/803 of query aligns to 236:826/921 of Q9FN05
- S517 (≠ E429) mutation to F: In psl5-1; Compromised defense response induced by the bacterial elicitor elongation factor Tu (EF-Tu).
- S599 (≠ N506) mutation to F: In rsw3; temperature-sensitive radial swelling of roots and reduction in cellulose production.
Q14697 Neutral alpha-glucosidase AB; Alpha-glucosidase 2; Glucosidase II subunit alpha; EC 3.2.1.207 from Homo sapiens (Human) (see 6 papers)
29% identity, 72% coverage: 150:727/803 of query aligns to 254:851/944 of Q14697
- R309 (≠ T201) to C: no effect on PKD1 and PKD2 localization to the cell surface; dbSNP:rs1063445
- T383 (= T262) to R: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs879255642
- R400 (≠ T279) to L: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs770519542
- D542 (= D424) mutation to N: Loss of activity.
- R590 (≠ E467) to P: found in a patient with polycystic liver disease; uncertain significance; dbSNP:rs1465649718
- H785 (≠ Y662) 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 (≠ Q693) to W: in PKD3; fails to promote PKD1 and PKD2 localization to the cell surface; dbSNP:rs879255643
- H850 (= H726) 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)
5hjoA Murine endoplasmic reticulum alpha-glucosidase ii with bound substrate analogue (see paper)
29% identity, 72% coverage: 150:727/803 of query aligns to 184:761/854 of 5hjoA
- binding D-glucal: D213 (= D175), F215 (≠ M177), W413 (= W387), M453 (≠ N425), D528 (= D495)
- binding 2-deoxy-alpha-D-arabino-hexopyranose: W311 (≠ M280), D339 (≠ S312), I340 (≠ S313), W450 (= W422), D452 (= D424), R512 (= R479), D528 (= D495), F561 (= F528), H586 (= H554)
5hjrA Murine endoplasmic reticulum alpha-glucosidase ii with bound covalent intermediate (see paper)
29% identity, 72% coverage: 150:727/803 of query aligns to 185:762/855 of 5hjrA
7kryA Co-crystal structure of alpha glucosidase with compound 11 (see paper)
27% identity, 87% coverage: 28:727/803 of query aligns to 56:761/854 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 (≠ M177), W311 (≠ M280), D339 (≠ S312), I340 (≠ S313), W411 (≠ Q385), C412 (≠ F386), W413 (= W387), W450 (= W422), D452 (= D424), F459 (≠ W431), D528 (= D495), F561 (= F528), H586 (= H554)
7kb8A Co-crystal structure of alpha glucosidase with compound 8 (see paper)
27% identity, 87% coverage: 28:727/803 of query aligns to 56:761/854 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 (≠ M177), W311 (≠ M280), D339 (≠ S312), I340 (≠ S313), W413 (= W387), W450 (= W422), D452 (= D424), F459 (≠ W431), R512 (= R479), D528 (= D495), F561 (= F528), H586 (= H554)
7kadA Co-crystal structure of alpha glucosidase with compound 6 (see paper)
27% identity, 87% coverage: 28:727/803 of query aligns to 56:761/854 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 (≠ M177), W311 (≠ M280), D339 (≠ S312), I340 (≠ S313), W413 (= W387), W450 (= W422), D452 (= D424), F459 (≠ W431), D528 (= D495), F561 (= F528), H586 (= H554)
7k9oA Co-crystal structure of alpha glucosidase with compound 3 (see paper)
27% identity, 87% coverage: 28:727/803 of query aligns to 56:761/854 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 (≠ M177), W311 (≠ M280), D339 (≠ S312), I340 (≠ S313), W413 (= W387), W450 (= W422), D452 (= D424), M453 (≠ N425), F459 (≠ W431), R512 (= R479), D528 (= D495), F561 (= F528), H586 (= H554)
7k9qA Co-crystal structure of alpha glucosidase with compound 4 (see paper)
27% identity, 87% coverage: 28:727/803 of query aligns to 56:760/853 of 7k9qA
- binding (1S,2S,3R,4S,5S)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: W310 (≠ M280), D338 (≠ S312), I339 (≠ S313), W449 (= W422), D451 (= D424), M452 (≠ N425), R511 (= R479), D527 (= D495), F560 (= F528), H585 (= H554)
7k9nA Co-crystal structure of alpha glucosidase with compound 2 (see paper)
27% identity, 87% coverage: 28:727/803 of query aligns to 56:760/853 of 7k9nA
- binding (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(9-methoxynonyl)amino]cyclohexane-1,2,3,4-tetrol: W310 (≠ M280), D338 (≠ S312), I339 (≠ S313), W412 (= W387), W449 (= W422), D451 (= D424), R511 (= R479), D527 (= D495), F560 (= F528), H585 (= H554), D589 (= D559)
5ieeA Murine endoplasmic reticulum alpha-glucosidase ii with 1- deoxynojirimycin (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 186:764/857 of 5ieeA
5iedA Murine endoplasmic reticulum alpha-glucosidase ii with castanospermine (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 186:764/857 of 5iedA
- binding castanospermine: W314 (≠ M280), D342 (≠ S312), I343 (≠ S313), W416 (= W387), W453 (= W422), D455 (= D424), R515 (= R479), W528 (= W492), D531 (= D495), F564 (= F528), H589 (= H554)
5h9oA Complex of murine endoplasmic reticulum alpha-glucosidase ii with d- glucose (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 186:764/857 of 5h9oA
5iefA Murine endoplasmic reticulum alpha-glucosidase ii with n-butyl-1- deoxynojirimycin (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 186:764/858 of 5iefA
- binding (2r,3r,4r,5s)-1-butyl-2-(hydroxymethyl)piperidine-3,4,5-triol: W314 (≠ M280), D342 (≠ S312), W453 (= W422), D455 (= D424), F462 (≠ W431), R515 (= R479), W528 (= W492), D531 (= D495), F564 (= F528), H589 (= H554)
7kb6A Co-crystal structure of alpha glucosidase with compound 7 (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 179:757/850 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 (≠ M177), W307 (≠ M280), D335 (≠ S312), I336 (≠ S313), W409 (= W387), W446 (= W422), D448 (= D424), F455 (≠ W431), R508 (= R479), D524 (= D495), F557 (= F528), H582 (= H554)
7k9tA Co-crystal structure of alpha glucosidase with compound 5 (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 179:757/850 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 (≠ M177), W307 (≠ M280), D335 (≠ S312), I336 (≠ S313), W409 (= W387), W446 (= W422), D448 (= D424), R508 (= R479), D524 (= D495), F557 (= F528), H582 (= H554)
Q8BHN3 Neutral alpha-glucosidase AB; Alpha-glucosidase 2; Glucosidase II subunit alpha; EC 3.2.1.207 from Mus musculus (Mouse) (see 3 papers)
28% identity, 72% coverage: 150:727/803 of query aligns to 254:851/944 of Q8BHN3
- D542 (= D424) active site, Nucleophile; mutation D->E,N: Loss of enzyme activity.
- D618 (= D495) active site, Proton donor; mutation to N: Loss of enzyme activity.
- C633 (≠ G510) modified: Disulfide link with 644
- C644 (≠ I521) modified: Disulfide link with 633
- R818 (≠ Q694) 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
7jtyA Co-crystal structure of alpha glucosidase with compound 1 (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 180:758/851 of 7jtyA
- binding (1S,2S,3R,4S,5S)-5-(butylamino)-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol: W308 (≠ M280), D336 (≠ S312), I337 (≠ S313), W410 (= W387), W447 (= W422), D449 (= D424), M450 (≠ N425), R509 (= R479), D525 (= D495), F558 (= F528), H583 (= H554)
5iegA Murine endoplasmic reticulum alpha-glucosidase ii with n-9'- methoxynonyl-1-deoxynojirimycin (see paper)
28% identity, 72% coverage: 150:727/803 of query aligns to 186:761/856 of 5iegA
- binding N-9'-methoxynonyl-1-deoxynojirimycin: F217 (≠ M177), W314 (≠ M280), D342 (≠ S312), I343 (≠ S313), W450 (= W422), D452 (= D424), R512 (= R479), W525 (= W492), D528 (= D495), F561 (= F528), H586 (= H554)
Query Sequence
>HSERO_RS20525 FitnessBrowser__HerbieS:HSERO_RS20525
MSMLHPPRFALQSSEGNHLCLKADTGAVIELFVLEEDIIRVLVLPEGKLQGPASWAVAPG
AEDVPLQGRDRRDLSGFALPSFALRTTPGQLQIETALIRLSIALEGGFCQWELRQEGQWQ
SVLADRPTQAYNFGYWDEQVYHYLRRQPEEMYFGLGERAGDMNRAGQSYEMRNIDAMGYS
ARNTDPLYKHIPFYITWLPKTGAGFGLFYDTLSDCRFDMGRELDNYHGHYRYFTAPHGDL
DYYFIASPGTPLAATRRFTWLTGRPAWMPKWGLGYSGSTMSYTDAPDAQVQMGQFIAKCR
EHDILCDSFHLSSGYTSIGPKRYVFHWNTEKFPDPHGFVRSYLDASIHLCANIKPCLLRD
HPQFEQARQAGLLICDSQGEPAWVQFWDEVGAYLDFTNPATLDWWRANVKQALLDYGVSA
TWNDNNEFEVWTGDAYAHGFGQQYPVRQAKVLQTMLMMQASRQAQLEAAPQRRPFLVSRS
GGAGMQRYVQTWSGDNYTSWETLRYNLKMGLGLALSGVSNIGHDIGGFSGPAPAPELLVR
WVAFGVFMPRFSIHSWNDDKTVNEPWMYPEVTAQIAALIKLRYRFIPYLYELLWQSTQDY
QPVLRPTFAEFPHDRRCLDECDDMMLGSAMLVAPVVEQGQTERRVYLPSGARWVSYWSGE
RYEGGQEISLPAPWDQPVMLLREGAVIPMNVAQQQFDVRADERAFLVVPYKEQGEASGAC
VEDDGHSQAWRDGEQGRWQVRARSDAAAVTLEVGREDRLPVAAETIDIFLPASEQRPVRA
TQARIVSEQRSQGWRRLTLALST
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