SitesBLAST
Comparing N515DRAFT_3770 FitnessBrowser__Dyella79:N515DRAFT_3770 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
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)
34% identity, 82% coverage: 36:392/433 of query aligns to 40:397/468 of P24058
- 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 (= T156) 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 (= H157) mutation to E: Loss of activity.
- R238 (≠ G234) 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 (= Y318) binding in chain A
- K325 (≠ R320) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q323) binding in chain A
- D330 (≠ S325) mutation to N: Loss of activity.
- K331 (= K326) binding in chain A; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 11 W→A: 98% decrease in catalytic efficiency.; W→F: 90% decrease in catalytic efficiency.; W→M: 99% decrease in catalytic efficiency.; W→R: 97% decrease in catalytic efficiency.; W→Y: 50% decrease in catalytic efficiency.
- 29 binding in chain A; S→A: 10% decrease in catalytic efficiency.
- 33 D→N: 99% decrease in catalytic efficiency.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
33% identity, 82% coverage: 36:392/433 of query aligns to 23:380/450 of 1k7wD
- active site: E71 (= E84), T144 (= T156), H145 (= H157), A266 (≠ S279), S267 (= S280), K272 (= K285), E279 (= E292)
- binding argininosuccinate: R98 (= R111), N99 (= N112), V102 (≠ I115), T144 (= T156), H145 (= H157), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
37% identity, 86% coverage: 14:385/433 of query aligns to 3:376/450 of 2e9fB
- active site: E71 (= E84), T146 (= T156), H147 (= H157), S268 (= S279), S269 (= S280), K274 (= K285), E281 (= E292)
- binding arginine: R98 (= R111), N99 (= N112), V102 (≠ I115), Y308 (= Y318), Q313 (= Q323), K316 (= K326)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
33% identity, 82% coverage: 36:392/433 of query aligns to 21:378/447 of 1hy0A
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
33% identity, 88% coverage: 13:391/433 of query aligns to 17:394/464 of P04424
- 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 (≠ A67) modified: N6-acetyllysine
- E73 (≠ D71) 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 (≠ A92) 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 (≠ A118) to E: in ARGINSA; severe
- V178 (≠ E175) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ I178) to S: in a breast cancer sample; somatic mutation
- R182 (≠ D179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G197) to V: in a breast cancer sample; somatic mutation
- R236 (= R233) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (≠ K235) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ N284) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R286) 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 (≠ A303) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q323) to L: in ARGINSA; severe
- V335 (≠ G332) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M357) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V379) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R382) to L: in ARGINSA; severe
- H388 (≠ Y385) to Q: in ARGINSA; severe
Sites not aligning to the query:
- 12 R → Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- 398 A → D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- 456 R → 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)
34% identity, 88% coverage: 14:395/433 of query aligns to 7:389/451 of 1tj7B
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
31% identity, 82% coverage: 36:392/433 of query aligns to 38:395/466 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)
33% identity, 86% coverage: 35:408/433 of query aligns to 21:387/418 of 6ienC
- binding arginine: R98 (= R111), N99 (= N112), V102 (≠ I115), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
- binding argininosuccinate: T144 (= T156), H145 (= H157), S266 (= S279), S267 (= S280), M269 (= M282), K272 (= K285)
- binding fumaric acid: S97 (= S110), R98 (= R111), N99 (= N112)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 81% coverage: 35:385/433 of query aligns to 21:374/454 of 6ienB
- binding argininosuccinate: S97 (= S110), R98 (= R111), N99 (= N112), T144 (= T156), H145 (= H157), S266 (= S279), S267 (= S280), M269 (= M282), K272 (= K285), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 81% coverage: 35:385/433 of query aligns to 21:372/452 of 6ienA
- binding argininosuccinate: R98 (= R111), N99 (= N112), V102 (≠ I115), T144 (= T156), H145 (= H157), Y304 (= Y318), Q309 (= Q323), K312 (= K326)
- binding fumaric acid: S266 (= S279), S267 (= S280), K270 (= K285), N272 (= N287)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
29% identity, 62% coverage: 26:295/433 of query aligns to 29:292/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
29% identity, 62% coverage: 26:295/433 of query aligns to 29:292/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
29% identity, 62% coverage: 26:295/433 of query aligns to 29:292/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
29% identity, 62% coverage: 26:295/433 of query aligns to 29:292/497 of 6g3fA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
23% identity, 72% coverage: 89:401/433 of query aligns to 71:387/427 of 2x75A
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)
24% identity, 56% coverage: 45:288/433 of query aligns to 32:271/431 of P12047
- H89 (= H106) mutation to Q: Abolishes enzyme activity.
- H141 (= H157) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ V227) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N287) mutation N->D,L: Abolishes enzyme activity.
Sites not aligning to the query:
- 301 mutation R->K,Q: Abolishes enzyme activity.
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
26% identity, 45% coverage: 98:294/433 of query aligns to 81:277/431 of Q9X0I0
- H141 (= H157) active site, Proton donor/acceptor
Query Sequence
>N515DRAFT_3770 FitnessBrowser__Dyella79:N515DRAFT_3770
MTQPLWQKSGIQIDARIMRFLAGDDVVLDREFFLHDITASKAHVEGLAKIGVVSADEAAA
LKRELDALAADFSAGDFVLDESYEDGHSAIEARLTERLGDAGRRVHTGRSRNDQILVATR
LWLKDQLAVLETHCRAIAEVCLERAAQPALPLPGYTHIQRAVVSSTAMWFAGFAEGFIDN
TLRARQTAALIDCNPLGTAAGYGVNLPLDREHTTQALGFARMQVSPVYAQLSRGKFEMAV
LEAIAAALLDVRRLAWDLSLFTTAEFGFVKLPSEYTTGSSIMPNKRNPDVVELLRASYAS
VAAARTEIEQLLSLPSGYQRDLQFSKGSLFHGCRHGLAALELVPDLLARMEWHEPAMRAA
IEPAMYATDVAIEQAAAGVPFRDAYRAAADAAASAGAGRTPEGSLAARVSPGAGHDLRLD
ELKARLAALTPGH
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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