SitesBLAST

SitesBLAST – Find functional sites

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 2 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

query
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Q3UDW8

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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

query
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Q68CP4

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P265 (≠ K27) to Q: likely benign variant; 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: likely benign variant; 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: 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; unknown pathological 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.

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