SitesBLAST
Comparing 202605 FitnessBrowser__MR1:202605 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 4 hits to proteins with known functional sites (download)
Q3UDW8 Heparan-alpha-glucosaminide N-acetyltransferase; Transmembrane protein 76; EC 2.3.1.78 from Mus musculus (Mouse) (see paper)
25% identity, 100% coverage: 1:395/395 of query aligns to 219:656/656 of Q3UDW8
Sites not aligning to the query:
- 157 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q68CP4 Heparan-alpha-glucosaminide N-acetyltransferase; Transmembrane protein 76; EC 2.3.1.78 from Homo sapiens (Human) (see 10 papers)
26% identity, 99% coverage: 5:395/395 of query aligns to 243:663/663 of Q68CP4
- P265 (≠ K27) to Q: in MPS3C; likely benign; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme
- G290 (≠ W63) to R: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- H297 (= H72) active site; mutation to A: Loss of enzymatic activity, but correctly targeted and processed.
- N301 (≠ H76) to K: in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity
- P311 (= P86) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- C333 (≠ L112) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
- R372 (= R148) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; to H: in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity
- C402 (≠ T170) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
- W431 (≠ L183) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- G452 (vs. gap) to S: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; to V: in MPS3C; shows practically no enzyme activity
- C462 (vs. gap) mutation to S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
- L473 (= L216) to P: in MPS3C; shows practically no enzyme activity
- H479 (vs. gap) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
- E499 (= E231) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- V509 (= V241) to L: in MPS3C; likely benign; no loss of enzymatic activity
- M510 (≠ N242) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- G514 (= G246) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- A517 (≠ V249) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- S546 (≠ G269) to F: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- K551 (≠ L278) to Q: in MPS3C; likely benign; no loss of enzymatic activity; dbSNP:rs73569592
- S567 (≠ T294) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- S569 (= S296) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
- D590 (= D317) to V: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
- P599 (≠ V325) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
- H633 (≠ V361) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
- A643 (= A371) to T: in RP73 and MPS3C; uncertain significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity; dbSNP:rs112029032
Sites not aligning to the query:
- 82 A → V: in MPS3C; shows practically no enzyme activity
- 104 C → F: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; loss of intralysosomal proteolytic cleavage
- 107 C→S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
- 141 L → P: in MPS3C; shows practically no enzyme activity
- 142 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 151 C→S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.
- 165 L → P: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
- 179 C→S: Loss of intralysosomal proteolytic cleavage and enzymatic activity.
- 236 L→A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209.
- 237 I→A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208.
8jl1A Membrane proteins
26% identity, 92% coverage: 32:395/395 of query aligns to 141:527/527 of 8jl1A
- binding acetyl coenzyme *a: R146 (= R37), M153 (≠ L55), N157 (≠ G59), V180 (≠ I84), F181 (= F85), F184 (= F88), S191 (≠ A95), S195 (= S99), K212 (= K120), R216 (= R121), V247 (= V152), L251 (≠ I156), S471 (≠ A335), I472 (= I336)
Sites not aligning to the query:
8jl4A Membrane proteins
26% identity, 92% coverage: 32:395/395 of query aligns to 147:533/533 of 8jl4A
- binding cholesterol: L307 (≠ W192), P309 (= P194)
- binding coenzyme a: V148 (≠ L33), D149 (= D34), R152 (= R37), M159 (≠ L55), F187 (= F85), F190 (= F88), M194 (≠ S92), S197 (≠ A95), S201 (= S99), K218 (= K120), R222 (= R121), V253 (= V152), L257 (≠ I156), S477 (≠ A335), Y481 (= Y339), K532 (≠ R394)
- binding ~{N}-[(2~{S},3~{R},4~{R},5~{S},6~{R})-6-(hydroxymethyl)-2-[[(2~{R},4~{R})-4-methyl-2-oxidanyl-3,4-dihydro-2~{H}-chromen-7-yl]oxy]-4,5-bis(oxidanyl)oxan-3-yl]ethanamide: N163 (≠ G59), Y164 (≠ W60), H174 (= H72), R249 (= R148), E369 (= E231), K433 (= K290), H484 (≠ S342), E485 (≠ S343), E488 (≠ D346)
Sites not aligning to the query:
Query Sequence
>202605 FitnessBrowser__MR1:202605
MSTTAPELAANVSINAQVATANNSQPKPRLMSLDALRGFDMFWILGGEALFGALLIFTGW
AGWQWGDTQMHHSEWHGFRLYDLIFPLFIFLSGVALGLSPKRLDKLPLHERLPVYRHGVK
RLFLLLLLGILYNHGWGTGAPVDPDKIRYASVLGRIAFAWFFAALLVWHTSLRTQVLVAV
GILVGYGAMQLWLPFPGGQAGVLSPTVSINAYVDSLLLPGVSYQGRMPDPEGVLSTLPAV
VNALAGVFVGHFIVKSHPKGEWAKVGLLGAAGGVCLALGWLLDAVIPVNKELWTSSFVLV
TSGWSMLLLALFYALVDVLKWQKLVFVFVVIGTNAIIIYLASSLVDWKYIAQSVFGGVIA
VLPEYAQPLGAVVSLLNVQWLVLYWMYRRKIFVRI
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