SitesBLAST
Comparing Ga0059261_2049 FitnessBrowser__Korea:Ga0059261_2049 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 20 (the maximum) hits to proteins with known functional sites (download)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
47% identity, 98% coverage: 9:456/456 of query aligns to 1:449/450 of 2e9fB
- active site: E71 (= E79), T146 (= T152), H147 (= H153), S268 (= S274), S269 (= S275), K274 (= K280), E281 (= E287)
- binding arginine: R98 (= R106), N99 (= N107), V102 (= V110), Y308 (= Y314), Q313 (= Q319), K316 (= K322)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
46% identity, 99% coverage: 5:455/456 of query aligns to 1:451/451 of 1tj7B
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
42% identity, 99% coverage: 1:452/456 of query aligns to 8:457/464 of P04424
- R12 (= R5) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D24) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ E44) mutation to N: 2-fold reduction in activity.
- K69 (≠ A62) modified: N6-acetyllysine
- E73 (≠ D66) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D80) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H82) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A87) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R88) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R106) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D113) to E: in ARGINSA; severe
- V178 (≠ E171) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ A174) to S: in a breast cancer sample; somatic mutation
- R182 (= R175) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G193) to V: in a breast cancer sample; somatic mutation
- R236 (= R229) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D230) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q279) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R281) 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 (= R290) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ C299) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q319) to L: in ARGINSA; severe
- V335 (≠ A328) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M353) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ I377) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R380) to L: in ARGINSA; severe
- H388 (= H383) to Q: in ARGINSA; severe
- A398 (= A393) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R451) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
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)
39% identity, 99% coverage: 1:451/456 of query aligns to 10:458/468 of P24058
- W11 (= W2) 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 (= S20) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D24) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D80) mutation to N: Loss of activity.
- N116 (= N107) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D108) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T152) 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 (= H153) mutation to E: Loss of activity.
- R238 (= R229) mutation to Q: Loss of activity.
- T281 (= T272) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S274) 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 (= N282) binding in chain B; mutation to L: Loss of activity.
- D293 (= D284) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E287) mutation to D: Loss of activity.
- Y323 (= Y314) binding in chain A
- K325 (= K316) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q319) binding in chain A
- D330 (= D321) mutation to N: Loss of activity.
- K331 (= K322) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
39% identity, 96% coverage: 13:451/456 of query aligns to 5:441/450 of 1k7wD
- active site: E71 (= E79), T144 (= T152), H145 (= H153), A266 (≠ S274), S267 (= S275), K272 (= K280), E279 (= E287)
- binding argininosuccinate: R98 (= R106), N99 (= N107), V102 (= V110), T144 (= T152), H145 (= H153), Y306 (= Y314), Q311 (= Q319), K314 (= K322)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
45% identity, 96% coverage: 10:449/456 of query aligns to 1:440/454 of 6ienB
- binding argininosuccinate: S97 (= S105), R98 (= R106), N99 (= N107), T144 (= T152), H145 (= H153), S266 (= S274), S267 (= S275), M269 (= M277), K272 (= K280), Y306 (= Y314), Q311 (= Q319), K314 (= K322)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
38% identity, 96% coverage: 13:451/456 of query aligns to 3:439/447 of 1hy0A
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
45% identity, 96% coverage: 10:449/456 of query aligns to 1:438/452 of 6ienA
- binding argininosuccinate: R98 (= R106), N99 (= N107), V102 (= V110), T144 (= T152), H145 (= H153), Y304 (= Y314), Q309 (= Q319), K312 (= K322)
- binding fumaric acid: S266 (= S274), S267 (= S275), K270 (= K280), N272 (= N282)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
36% identity, 99% coverage: 1:451/456 of query aligns to 8:456/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 96% coverage: 10:449/456 of query aligns to 1:404/418 of 6ienC
- binding arginine: R98 (= R106), N99 (= N107), V102 (= V110), Y306 (= Y314), Q311 (= Q319), K314 (= K322)
- binding argininosuccinate: T144 (= T152), H145 (= H153), S266 (= S274), S267 (= S275), M269 (= M277), K272 (= K280)
- binding fumaric acid: S97 (= S105), R98 (= R106), N99 (= N107)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
36% identity, 86% coverage: 18:409/456 of query aligns to 33:408/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
36% identity, 86% coverage: 18:409/456 of query aligns to 33:408/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
36% identity, 86% coverage: 18:409/456 of query aligns to 33:408/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
36% identity, 86% coverage: 18:409/456 of query aligns to 33:408/497 of 6g3fA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
29% identity, 58% coverage: 92:356/456 of query aligns to 125:388/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
29% identity, 58% coverage: 92:356/456 of query aligns to 124:387/462 of 3r6qA
Sites not aligning to the query:
P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
26% identity, 50% coverage: 89:318/456 of query aligns to 77:303/431 of P12047
- H89 (= H101) mutation to Q: Abolishes enzyme activity.
- H141 (= H153) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ A225) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N282) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K316) mutation R->K,Q: Abolishes enzyme activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
23% identity, 60% coverage: 88:361/456 of query aligns to 75:348/427 of 2x75A
Sites not aligning to the query:
3oceA Crystal structure of fumarate lyase:delta crystallin from brucella melitensis bound to cobalt
27% identity, 59% coverage: 100:367/456 of query aligns to 134:411/461 of 3oceA
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
25% identity, 51% coverage: 71:303/456 of query aligns to 99:347/464 of 7c18B
- binding fumaric acid: T100 (≠ V72), S139 (= S105), S140 (≠ R106), N141 (= N107), T187 (= T152), H188 (= H153), C318 (≠ S274), S319 (= S275), M321 (= M277), K324 (= K280), N326 (= N282)
Query Sequence
>Ga0059261_2049 FitnessBrowser__Korea:Ga0059261_2049
MWGGRFAEGPSSVMREINASIPFDKRMWRQDIAGSKAHVAMLGEQGIVDAADAATISAGL
DAVAADYERDGVPEDLALEDIHMLTEARLAEKIGPVAGRLHTARSRNDQVATDFRLWVRD
ATDQVLAALAALQDALLARADEHAGSVMPGFTHLQSAQPVTLGHHLMAYFEMIARDVSRF
ADARARGNRCPLGSAALAGTGFPLDRDATAAALGFDGPTRNSLDAVSDRDFALDYLMAAA
QCALHLSRLAEEFVIWASQPFGFVKLSDQWSTGSSIMPQKRNPDAAELVRGHSGRIVGCL
TSLMITMKGLPLAYSKDMQDDKPPVFEAHDLLALSIAAMTGMVESAQFRTDRMRGLAESG
FATATDLADWLVREGGIPFREAHHITGRAVAAAEAKNVRLDQLELADLQAIDQRIDERVF
GVLTVDASVASRISFGGTAPVRVREAIAAARAARGV
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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