SitesBLAST

Comparing Pf6N2E2_4429 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4429 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
52% identity, 93% coverage: 19:451/464 of query aligns to 3:437/450 of 2e9fB

• active site: E71 (= E87), T146 (= T160), H147 (= H161), S268 (= S282), S269 (= S283), K274 (= K288), E281 (= E295)
• binding arginine: R98 (= R114), N99 (= N115), V102 (= V118), Y308 (= Y322), Q313 (= Q327), K316 (= K330)

1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
49% identity, 97% coverage: 13:461/464 of query aligns to 1:450/451 of 1tj7B

• active site: H150 (= H161), S271 (= S282), K277 (= K288), E284 (= E295)
• binding phosphate ion: S271 (= S282), M274 (= M285), K277 (= K288)

P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
44% identity, 96% coverage: 10:454/464 of query aligns to 11:454/468 of P24058

• W11 (= W10) mutation to A: 98% decrease in catalytic efficiency.; mutation to F: 90% decrease in catalytic efficiency.; mutation to M: 99% decrease in catalytic efficiency.; mutation to R: 97% decrease in catalytic efficiency.; mutation to Y: 50% decrease in catalytic efficiency.
• S29 (= S28) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (= D32) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D88) mutation to N: Loss of activity.
• N116 (= N115) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D116) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T160) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
• H162 (= H161) mutation to E: Loss of activity.
• R238 (= R237) mutation to Q: Loss of activity.
• T281 (= T280) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S282) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
• N291 (= N290) binding in chain B; mutation to L: Loss of activity.
• D293 (= D292) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E295) mutation to D: Loss of activity.
• Y323 (= Y322) binding in chain A
• K325 (= K324) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (= Q327) binding in chain A
• D330 (= D329) mutation to N: Loss of activity.
• K331 (= K330) binding in chain A; mutation to Q: Loss of activity.

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
43% identity, 99% coverage: 5:464/464 of query aligns to 4:462/464 of P04424

• R12 (= R13) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (= D32) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (= K52) mutation to N: 2-fold reduction in activity.
• K69 (≠ T70) modified: N6-acetyllysine
• E73 (= E74) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D88) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H90) mutation to Q: 10-fold reduction in activity.
• R94 (≠ A95) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (= R96) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R114) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D121) to E: in ARGINSA; severe
• V178 (≠ E179) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ S182) to S: in a breast cancer sample; somatic mutation
• R182 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R187) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G201) to V: in a breast cancer sample; somatic mutation
• R236 (= R237) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D238) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q287) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K289) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
• R297 (= R298) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ A307) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (= Q327) to L: in ARGINSA; severe
• V335 (≠ A336) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (= M361) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ L384) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R387) to L: in ARGINSA; severe
• H388 (= H390) to Q: in ARGINSA; severe
• A398 (≠ G400) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
• R456 (≠ Q458) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
43% identity, 94% coverage: 19:454/464 of query aligns to 3:437/450 of 1k7wD

• active site: E71 (= E87), T144 (= T160), H145 (= H161), A266 (≠ S282), S267 (= S283), K272 (= K288), E279 (= E295)
• binding argininosuccinate: R98 (= R114), N99 (= N115), V102 (= V118), T144 (= T160), H145 (= H161), Y306 (= Y322), Q311 (= Q327), K314 (= K330)

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 94% coverage: 19:454/464 of query aligns to 1:435/447 of 1hy0A

• active site: E69 (= E87), T142 (= T160), H143 (= H161), S264 (= S282), S265 (= S283), K270 (= K288), E277 (= E295)
• binding sulfate ion: S264 (= S282), M267 (= M285), N272 (= N290)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
40% identity, 97% coverage: 10:461/464 of query aligns to 9:459/466 of P02521

Sites not aligning to the query:

• 2 modified: Blocked amino end (Ala)

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
45% identity, 94% coverage: 17:450/464 of query aligns to 1:434/454 of 6ienB

• binding argininosuccinate: S97 (= S113), R98 (= R114), N99 (= N115), T144 (= T160), H145 (= H161), S266 (= S282), S267 (= S283), M269 (= M285), K272 (= K288), Y306 (= Y322), Q311 (= Q327), K314 (= K330)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
45% identity, 94% coverage: 17:450/464 of query aligns to 1:432/452 of 6ienA

• binding argininosuccinate: R98 (= R114), N99 (= N115), V102 (= V118), T144 (= T160), H145 (= H161), Y304 (= Y322), Q309 (= Q327), K312 (= K330)
• binding fumaric acid: S266 (= S282), S267 (= S283), K270 (= K288), N272 (= N290)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 94% coverage: 17:450/464 of query aligns to 1:398/418 of 6ienC

• binding arginine: R98 (= R114), N99 (= N115), V102 (= V118), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
• binding argininosuccinate: T144 (= T160), H145 (= H161), S266 (= S282), S267 (= S283), M269 (= M285), K272 (= K288)
• binding fumaric acid: S97 (= S113), R98 (= R114), N99 (= N115)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
32% identity, 94% coverage: 19:454/464 of query aligns to 25:454/496 of 6g3iA