SitesBLAST

Comparing Pf6N2E2_1798 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1798 to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
53% identity, 93% coverage: 17:459/475 of query aligns to 1:444/454 of 6ienB

• binding argininosuccinate: H73 (= H89), S97 (= S112), R98 (= R113), N99 (= N114), V102 (≠ T117), T144 (= T159), H145 (= H160), S266 (= S281), S267 (= S282), M269 (= M284), K272 (= K287), N274 (= N289), Y306 (= Y321), Q311 (≠ S326), K314 (= K329)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
53% identity, 93% coverage: 17:459/475 of query aligns to 1:442/452 of 6ienA

• binding argininosuccinate: S97 (= S112), R98 (= R113), N99 (= N114), V102 (≠ T117), T144 (= T159), H145 (= H160), Y304 (= Y321), Q309 (≠ S326), K312 (= K329)
• binding fumaric acid: S266 (= S281), S267 (= S282), K270 (= K287), N272 (= N289)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
49% identity, 93% coverage: 17:459/475 of query aligns to 1:408/418 of 6ienC

• binding arginine: R98 (= R113), N99 (= N114), V102 (≠ T117), Y306 (= Y321), R308 (= R323), L310 (= L325), Q311 (≠ S326), K314 (= K329)
• binding argininosuccinate: T144 (= T159), H145 (= H160), S266 (= S281), S267 (= S282), M269 (= M284), K272 (= K287), N274 (= N289)
• binding fumaric acid: S97 (= S112), R98 (= R113), N99 (= N114)

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)
38% identity, 97% coverage: 6:465/475 of query aligns to 8:466/468 of P24058

• W11 (= W9) 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 (≠ C27) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (≠ Y31) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D87) mutation to N: Loss of activity.
• N116 (= N114) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D115) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T159) 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 (= H160) mutation to E: Loss of activity.
• R238 (= R236) mutation to Q: Loss of activity.
• T281 (= T279) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S281) 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 (= N289) binding in chain B; mutation to L: Loss of activity.
• D293 (= D291) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E294) mutation to D: Loss of activity.
• Y323 (= Y321) binding in chain A
• K325 (≠ R323) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (≠ S326) binding in chain A
• D330 (= D328) mutation to N: Loss of activity.
• K331 (= K329) binding in chain A; mutation to Q: Loss of activity.

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
39% identity, 91% coverage: 33:465/475 of query aligns to 18:449/450 of 1k7wD

• active site: E71 (= E86), T144 (= T159), H145 (= H160), A266 (≠ S281), S267 (= S282), K272 (= K287), E279 (= E294)
• binding argininosuccinate: R98 (= R113), N99 (= N114), V102 (≠ T117), T144 (= T159), H145 (= H160), Y306 (= Y321), Q311 (≠ S326), K314 (= K329)

Sites not aligning to the query:

• binding argininosuccinate: 12

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
39% identity, 98% coverage: 1:464/475 of query aligns to 1:463/464 of P04424

• R12 (= R12) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (≠ Y31) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (≠ R51) mutation to N: 2-fold reduction in activity.
• K69 (≠ R69) modified: N6-acetyllysine
• E73 (≠ D73) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D87) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H89) mutation to Q: 10-fold reduction in activity.
• R94 (= R94) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (≠ L95) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R113) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D120) to E: in ARGINSA; severe
• V178 (≠ Q178) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ L181) to S: in a breast cancer sample; somatic mutation
• R182 (= R182) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R186) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G200) to V: in a breast cancer sample; somatic mutation
• R236 (= R236) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D237) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q286) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (= K288) 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 (= R297) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ N306) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (≠ S326) to L: in ARGINSA; severe
• V335 (≠ S335) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (≠ L360) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ V383) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (≠ K386) to L: in ARGINSA; severe
• H388 (= H389) to Q: in ARGINSA; severe
• A398 (≠ C399) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
• R456 (≠ K457) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
38% identity, 91% coverage: 33:465/475 of query aligns to 16:447/447 of 1hy0A

• active site: E69 (= E86), T142 (= T159), H143 (= H160), S264 (= S281), S265 (= S282), K270 (= K287), E277 (= E294)
• binding sulfate ion: S264 (= S281), M267 (= M284), K270 (= K287), N272 (= N289)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
37% identity, 98% coverage: 1:465/475 of query aligns to 1:464/466 of P02521

• A2 (= A2) modified: Blocked amino end (Ala)

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
44% identity, 88% coverage: 38:453/475 of query aligns to 23:440/450 of 2e9fB

• active site: E71 (= E86), T146 (= T159), H147 (= H160), S268 (= S281), S269 (= S282), K274 (= K287), E281 (= E294)
• binding arginine: D72 (= D87), R98 (= R113), N99 (= N114), V102 (≠ T117), Y308 (= Y321), Q313 (≠ S326), K316 (= K329)

1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
40% identity, 89% coverage: 32:453/475 of query aligns to 21:443/451 of 1tj7B

• active site: H150 (= H160), S271 (= S281), K277 (= K287), E284 (= E294)
• binding phosphate ion: S271 (= S281), M274 (= M284), K277 (= K287), N279 (= N289)

1dcnB Inactive mutant h162n of delta 2 crystallin with bound argininosuccinate (see paper)
35% identity, 91% coverage: 33:464/475 of query aligns to 16:418/418 of 1dcnB