SitesBLAST
Comparing Echvi_3852 FitnessBrowser__Cola:Echvi_3852 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
36% identity, 82% coverage: 25:388/444 of query aligns to 19:383/451 of 1tj7B
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
38% identity, 82% coverage: 25:388/444 of query aligns to 15:380/450 of 2e9fB
- active site: E71 (= E81), T146 (= T154), H147 (= H155), S268 (= S277), S269 (= S278), K274 (= K283), E281 (= E290)
- binding arginine: R98 (= R108), N99 (= N109), V102 (= V112), Y308 (= Y317), Q313 (= Q322), K316 (= K325)
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)
32% identity, 87% coverage: 2:388/444 of query aligns to 9:394/468 of P24058
- W11 (= W4) 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 (≠ D22) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D26) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D82) mutation to N: Loss of activity.
- N116 (= N109) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D110) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T154) 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 (= H155) mutation to E: Loss of activity.
- R238 (= R231) mutation to Q: Loss of activity.
- T281 (= T275) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S277) 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 (= N285) binding in chain B; mutation to L: Loss of activity.
- D293 (= D287) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E290) mutation to D: Loss of activity.
- Y323 (= Y317) binding in chain A
- K325 (≠ R319) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q322) binding in chain A
- D330 (≠ L324) mutation to N: Loss of activity.
- K331 (= K325) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
33% identity, 82% coverage: 25:388/444 of query aligns to 15:377/450 of 1k7wD
- active site: E71 (= E81), T144 (= T154), H145 (= H155), A266 (≠ S277), S267 (= S278), K272 (= K283), E279 (= E290)
- binding argininosuccinate: R98 (= R108), N99 (= N109), V102 (= V112), T144 (= T154), H145 (= H155), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
33% identity, 82% coverage: 25:388/444 of query aligns to 30:392/464 of P04424
- D31 (= D26) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ S46) mutation to N: 2-fold reduction in activity.
- K69 (≠ D64) modified: N6-acetyllysine
- E73 (= E68) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D82) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H84) mutation to Q: 10-fold reduction in activity.
- R94 (≠ F89) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ L90) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R108) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D115) to E: in ARGINSA; severe
- V178 (≠ E173) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ A176) to S: in a breast cancer sample; somatic mutation
- R182 (≠ E177) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (≠ L181) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G195) to V: in a breast cancer sample; somatic mutation
- R236 (= R231) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (≠ G232) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ H282) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K284) 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 (= R293) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ G302) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q322) to L: in ARGINSA; severe
- V335 (≠ D331) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L356) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (= M378) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R381) to L: in ARGINSA; severe
- H388 (≠ Y384) 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
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
31% identity, 81% coverage: 29:388/444 of query aligns to 17:375/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
32% identity, 84% coverage: 16:388/444 of query aligns to 12:392/466 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)
34% identity, 84% coverage: 25:399/444 of query aligns to 14:388/418 of 6ienC
- binding arginine: R98 (= R108), N99 (= N109), V102 (= V112), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
- binding argininosuccinate: T144 (= T154), H145 (= H155), S266 (= S277), S267 (= S278), M269 (= M280), K272 (= K283)
- binding fumaric acid: S97 (= S107), R98 (= R108), N99 (= N109)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
34% identity, 81% coverage: 25:385/444 of query aligns to 14:375/454 of 6ienB
- binding argininosuccinate: S97 (= S107), R98 (= R108), N99 (= N109), T144 (= T154), H145 (= H155), S266 (= S277), S267 (= S278), M269 (= M280), K272 (= K283), Y306 (= Y317), Q311 (= Q322), K314 (= K325)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
33% identity, 81% coverage: 25:385/444 of query aligns to 14:373/452 of 6ienA
- binding argininosuccinate: R98 (= R108), N99 (= N109), V102 (= V112), T144 (= T154), H145 (= H155), Y304 (= Y317), Q309 (= Q322), K312 (= K325)
- binding fumaric acid: S266 (= S277), S267 (= S278), K270 (= K283), N272 (= N285)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
29% identity, 61% coverage: 31:303/444 of query aligns to 37:301/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
29% identity, 61% coverage: 31:303/444 of query aligns to 37:301/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
29% identity, 61% coverage: 31:303/444 of query aligns to 37:301/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
29% identity, 61% coverage: 31:303/444 of query aligns to 37:301/496 of 6g3iA
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, 54% coverage: 84:321/444 of query aligns to 68:303/431 of P12047
- H89 (= H103) mutation to Q: Abolishes enzyme activity.
- H141 (= H155) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ I225) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N285) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R319) mutation R->K,Q: Abolishes enzyme activity.
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
26% identity, 45% coverage: 145:342/444 of query aligns to 160:360/476 of A0A0K2JL82
- R201 (≠ A189) binding fumarate
- H253 (vs. gap) mutation to A: Loss of activity.
- S302 (= S277) mutation to A: Loss of activity.
- K308 (= K283) binding fumarate; mutation to A: Loss of activity.
- N310 (= N285) binding fumarate; mutation to A: Loss of activity.
- R341 (≠ N312) mutation to A: Loss of activity.
Sites not aligning to the query:
- 93 N→A: Slight decrease in activity.
- 125 mutation D->N,V: Almost loss of activity.
- 137 binding fumarate
- 140 binding fumarate
5hw2A Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with fumaric acid
37% identity, 18% coverage: 96:173/444 of query aligns to 82:160/419 of 5hw2A
Sites not aligning to the query:
4eeiB Crystal structure of adenylosuccinate lyase from francisella tularensis complexed with amp and succinate
37% identity, 18% coverage: 96:173/444 of query aligns to 82:160/423 of 4eeiB
Sites not aligning to the query:
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)
21% identity, 75% coverage: 53:384/444 of query aligns to 35:372/431 of Q9X0I0
- H141 (= H155) active site, Proton donor/acceptor
Query Sequence
>Echvi_3852 FitnessBrowser__Cola:Echvi_3852
MKLWQKNTTSTKEVEQFTIGRDPEFDIVLAPFDVLGSLAHATMLESIDLLTKEELAILKK
GLKDIYQEIQEGTFTIDPGVEDVHSQVEFLLTERYGDVGKKLHSGRSRNDQVAVDLKLYY
RAVIQEVLDDAKALFDLLLTLAEKHQNDLMPGYTHTQLAMPSSFGLWFGAMAESLAEDME
LWLAAYNLADRNPLGSAAGYGSSFPLNRTMTTRLLGFKDMHYNVINAQNNRGKTEKAIAF
AMAGMAGTLNRLSADIIIFMNQHFGFVKFPDNLTTGSSIMPHKKNPDVFELIRAKANQIQ
SGPQNLMMQMTNTTTGYHRDLQLLKETTFPDFEKLKDCLQITKFMLEHIEIKPDILEDKF
YKHLFSVEVVNDLVLQGMPFRDAYKKVGLDIESDDFAPDHTVNHSHEGSIGQLCLDEIRT
KMETALAKFDFSAIETSYQKLLEA
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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