SitesBLAST
Comparing 8499269 FitnessBrowser__Miya:8499269 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
50% identity, 95% coverage: 17:453/460 of query aligns to 4:442/450 of 2e9fB
- active site: E71 (= E84), T146 (= T157), H147 (= H158), S268 (= S279), S269 (= S280), K274 (= K285), E281 (= E292)
- binding arginine: R98 (= R111), N99 (= N112), V102 (= V115), Y308 (= Y319), Q313 (= Q324), K316 (= K327)
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)
43% identity, 98% coverage: 5:454/460 of query aligns to 9:457/468 of P24058
- W11 (= W7) 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 (= S25) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D29) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D85) mutation to N: Loss of activity.
- N116 (= N112) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D113) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T157) 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 (= H158) mutation to E: Loss of activity.
- R238 (= R234) mutation to Q: Loss of activity.
- T281 (= T277) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S279) 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 (= N287) binding in chain B; mutation to L: Loss of activity.
- D293 (= D289) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E292) mutation to D: Loss of activity.
- Y323 (= Y319) binding in chain A
- K325 (≠ R321) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q324) binding in chain A
- D330 (= D326) mutation to N: Loss of activity.
- K331 (= K327) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
43% identity, 96% coverage: 14:454/460 of query aligns to 1:440/450 of 1k7wD
- active site: E71 (= E84), T144 (= T157), H145 (= H158), A266 (≠ S279), S267 (= S280), K272 (= K285), E279 (= E292)
- binding argininosuccinate: R98 (= R111), N99 (= N112), V102 (= V115), T144 (= T157), H145 (= H158), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 99% coverage: 5:459/460 of query aligns to 7:460/464 of P04424
- R12 (= R10) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D29) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (= K49) mutation to N: 2-fold reduction in activity.
- K69 (≠ M67) modified: N6-acetyllysine
- E73 (= E71) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D85) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H87) mutation to Q: 10-fold reduction in activity.
- R94 (≠ S92) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R93) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R111) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D118) to E: in ARGINSA; severe
- V178 (≠ W176) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ R179) to S: in a breast cancer sample; somatic mutation
- R182 (= R180) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R184) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G198) to V: in a breast cancer sample; somatic mutation
- R236 (= R234) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D235) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q284) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K286) 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 (= R295) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A304) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q324) to L: in ARGINSA; severe
- V335 (≠ C333) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M358) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ I381) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R384) to L: in ARGINSA; severe
- H388 (= H387) to Q: in ARGINSA; severe
- A398 (= A397) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ S455) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
45% identity, 96% coverage: 10:452/460 of query aligns to 1:444/451 of 1tj7B
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 99% coverage: 5:460/460 of query aligns to 7:461/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 95% coverage: 18:454/460 of query aligns to 3:438/447 of 1hy0A
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
45% identity, 93% coverage: 23:451/460 of query aligns to 9:438/454 of 6ienB
- binding argininosuccinate: S97 (= S110), R98 (= R111), N99 (= N112), T144 (= T157), H145 (= H158), S266 (= S279), S267 (= S280), M269 (= M282), K272 (= K285), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 93% coverage: 23:451/460 of query aligns to 9:436/452 of 6ienA
- binding argininosuccinate: R98 (= R111), N99 (= N112), V102 (= V115), T144 (= T157), H145 (= H158), Y304 (= Y319), Q309 (= Q324), K312 (= K327)
- binding fumaric acid: S266 (= S279), S267 (= S280), K270 (= K285), N272 (= N287)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
45% identity, 79% coverage: 23:387/460 of query aligns to 9:374/418 of 6ienC
- binding arginine: R98 (= R111), N99 (= N112), V102 (= V115), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
- binding argininosuccinate: T144 (= T157), H145 (= H158), S266 (= S279), S267 (= S280), M269 (= M282), K272 (= K285)
- binding fumaric acid: S97 (= S110), R98 (= R111), N99 (= N112)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
33% identity, 96% coverage: 10:451/460 of query aligns to 6:454/496 of 6g3iA