SitesBLAST

G290 (≠ T29) to R: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
H297 (= H39) active site; mutation to A: Loss of enzymatic activity, but correctly targeted and processed.
N301 (= N43) to K: in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity
P311 (= P53) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
C333 (= C70) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
R372 (= R131) 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 (≠ L161) mutation to S: No loss of intralysosomal proteolytic cleavage and enzymatic activity.
W431 (≠ F170) 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 (≠ T193) to P: in MPS3C; shows practically no enzyme activity
H479 (≠ M199) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
E499 (= E208) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
V509 (≠ A218) to L: in MPS3C; likely benign; no loss of enzymatic activity
M510 (≠ Q219) to K: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
G514 (= G223) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
A517 (≠ I226) to E: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
S546 (≠ L251) to F: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
K551 (≠ L256) to Q: in MPS3C; likely benign; no loss of enzymatic activity; dbSNP:rs73569592
S567 (≠ T269) to C: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum
S569 (= S271) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
D590 (= D292) to V: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
P599 (≠ T302) to L: in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity
H633 (≠ Y339) mutation to A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.
A643 (≠ L362) 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.
265 P → Q: in MPS3C; likely benign; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme

8jl4A Membrane proteins
27% identity, 98% coverage: 9:381/381 of query aligns to 147:533/533 of 8jl4A

query
sites
8jl4A

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binding cholesterol: L307 (vs. gap), P309 (vs. gap)
binding coenzyme a: V148 (≠ L10), D149 (= D11), R152 (= R14), M159 (= M21), F187 (= F52), F190 (= F55), M194 (= M59), S197 (= S62), S201 (= S66), K218 (= K81), R222 (= R85), V253 (= V135), L257 (= L139), S477 (≠ P310), Y481 (= Y314), K532 (= K380)
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 (= N25), Y164 (≠ T26), H174 (= H39), R249 (= R131), E369 (= E208), K433 (= K265), H484 (≠ S317), E485 (= E318), E488 (≠ A321)

Sites not aligning to the query:

binding coenzyme a: 144, 145

8jl1A Membrane proteins
27% identity, 98% coverage: 9:381/381 of query aligns to 141:527/527 of 8jl1A

query
sites
8jl1A

A

S

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V

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L

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x
S

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I

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F

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binding acetyl coenzyme *a: R146 (= R14), M153 (= M21), N157 (= N25), V180 (≠ I51), F181 (= F52), F184 (= F55), S191 (= S62), S195 (= S66), K212 (= K81), R216 (= R85), V247 (= V135), L251 (= L139), S471 (≠ P310), I472 (≠ L311)

Sites not aligning to the query:

binding acetyl coenzyme *a: 138, 139

Query Sequence

>WP_009125699.1 NCBI__GCF_000195635.1:WP_009125699.1
MKNNQRLVALDVMRGLTIAGMILVNTPETWSYVYAPLQHARWNGLTPTDVIFPFFLFMMG
VSMYISLKKCSFHLSSHLLMKIIRRSLILFLIGTAIYALATFLGTLRDACRQPGFEGNPW
KEAFASLPGTRIPGVLQRLGVCYGIGSIIVLTCRHRYIPHLAGGILAGYFLILLFGNGFV
HSPENILSVVDRTLFGDNMINDGGIDPEGALSTLPSIAQVLIGFCIGKICIETPDMREKL
NKIFLYGSLMLIVGWLFSYGCPLNKRVWTPSFVLVTCGFACLLLGILIWYIDLRKVYKQT
WTFEVFGVNPLFCYVLSEVLAILVDYLPLHSATLHERFYSGFLSNCFGDNEWTSFLYAFS
LLCSVWLIGVLLYKKKIYIKI

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