SitesBLAST
Comparing 3609679 FitnessBrowser__Dino:3609679 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
52% identity, 97% coverage: 17:463/463 of query aligns to 1:448/450 of 2e9fB
- active site: E71 (= E87), T146 (= T160), H147 (= H161), S268 (= S282), S269 (= S283), K274 (= K288), E281 (= E295)
- binding arginine: R98 (= R114), N99 (= N115), V102 (= V118), Y308 (= Y322), Q313 (= Q327), K316 (= K330)
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)
45% identity, 99% coverage: 2:460/463 of query aligns to 3:459/468 of P24058
- W11 (= W10) 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 (= S28) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D32) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D88) mutation to N: Loss of activity.
- N116 (= N115) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D116) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T160) 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 (= H161) mutation to E: Loss of activity.
- R238 (= R237) mutation to Q: Loss of activity.
- T281 (= T280) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S282) 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 (= N290) binding in chain B; mutation to L: Loss of activity.
- D293 (= D292) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E295) mutation to D: Loss of activity.
- Y323 (= Y322) binding in chain A
- K325 (= K324) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q327) binding in chain A
- D330 (= D329) mutation to N: Loss of activity.
- K331 (= K330) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
45% identity, 95% coverage: 19:460/463 of query aligns to 3:442/450 of 1k7wD
- active site: E71 (= E87), T144 (= T160), H145 (= H161), A266 (≠ S282), S267 (= S283), K272 (= K288), E279 (= E295)
- binding argininosuccinate: R98 (= R114), N99 (= N115), V102 (= V118), T144 (= T160), H145 (= H161), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
45% identity, 98% coverage: 4:455/463 of query aligns to 3:452/464 of P04424
- R12 (= R13) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D32) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ Q52) mutation to N: 2-fold reduction in activity.
- K69 (≠ T70) modified: N6-acetyllysine
- E73 (= E74) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D88) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H90) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A95) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R96) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R114) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D121) to E: in ARGINSA; severe
- V178 (≠ E179) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ A182) to S: in a breast cancer sample; somatic mutation
- R182 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R187) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G201) to V: in a breast cancer sample; somatic mutation
- R236 (= R237) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D238) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q287) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K289) 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 (= R298) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A307) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q327) to L: in ARGINSA; severe
- V335 (≠ A336) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L361) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ L385) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R388) to L: in ARGINSA; severe
- H388 (= H391) to Q: in ARGINSA; severe
- A398 (= A401) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
Sites not aligning to the query:
- 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)
43% identity, 95% coverage: 19:460/463 of query aligns to 1:440/447 of 1hy0A
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
46% identity, 97% coverage: 13:463/463 of query aligns to 1:451/451 of 1tj7B
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 99% coverage: 4:462/463 of query aligns to 3:459/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 95% coverage: 18:455/463 of query aligns to 1:438/454 of 6ienB
- binding argininosuccinate: S97 (= S113), R98 (= R114), N99 (= N115), T144 (= T160), H145 (= H161), S266 (= S282), S267 (= S283), M269 (= M285), K272 (= K288), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
43% identity, 95% coverage: 18:455/463 of query aligns to 1:436/452 of 6ienA
- binding argininosuccinate: R98 (= R114), N99 (= N115), V102 (= V118), T144 (= T160), H145 (= H161), Y304 (= Y322), Q309 (= Q327), K312 (= K330)
- binding fumaric acid: S266 (= S282), S267 (= S283), K270 (= K288), N272 (= N290)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 95% coverage: 18:455/463 of query aligns to 1:402/418 of 6ienC
- binding arginine: R98 (= R114), N99 (= N115), V102 (= V118), Y306 (= Y322), Q311 (= Q327), K314 (= K330)
- binding argininosuccinate: T144 (= T160), H145 (= H161), S266 (= S282), S267 (= S283), M269 (= M285), K272 (= K288)
- binding fumaric acid: S97 (= S113), R98 (= R114), N99 (= N115)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
35% identity, 89% coverage: 44:455/463 of query aligns to 44:454/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
35% identity, 89% coverage: 44:455/463 of query aligns to 44:454/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
35% identity, 89% coverage: 44:455/463 of query aligns to 44:454/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
35% identity, 89% coverage: 44:455/463 of query aligns to 44:454/496 of 6g3iA
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
26% identity, 59% coverage: 40:311/463 of query aligns to 33:344/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
26% identity, 59% coverage: 40:311/463 of query aligns to 32:343/462 of 3r6qA
Sites not aligning to the query:
P05042 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Escherichia coli (strain K12) (see 4 papers)
26% identity, 60% coverage: 34:311/463 of query aligns to 34:347/467 of P05042
- R126 (vs. gap) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (vs. gap) mutation to D: No effect.
- H129 (≠ E103) mutation to N: No effect on fumarase activity and essentially same conformation compared to the wild-type, but appears to dramatically reduce binding of ligands at the B-site.
- HPND 129:132 (≠ EPAG 103:106) binding in site B
- SSN 139:141 (≠ SRN 113:115) binding
- H188 (= H161) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (≠ S279) mutation to Q: There is essentially no effect on the affinity values for both S-malate and fumarate. In contrast, the catalytic efficiency values have been lowered by 10-fold in both directions.
1fupA Fumarase with bound pyromellitic acid (see paper)
26% identity, 60% coverage: 34:311/463 of query aligns to 30:343/455 of 1fupA
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
26% identity, 60% coverage: 34:311/463 of query aligns to 31:344/456 of 1fuqA
- active site: N104 (= N92), T184 (= T160), H185 (= H161), S315 (= S282), K321 (= K288), E328 (= E295)
- binding citric acid: T97 (≠ A85), S136 (= S113), S137 (≠ R114), N138 (= N115)
- binding 3-trimethylsilylsuccinic acid: R123 (vs. gap), H126 (≠ E103), P127 (= P104), N128 (≠ A105), D129 (≠ G106)
1fuoA FumarasE C with bound citrate (see paper)
26% identity, 60% coverage: 34:311/463 of query aligns to 31:344/456 of 1fuoA
Query Sequence
>3609679 FitnessBrowser__Dino:3609679
MSDTKSNAMWGGRFAAGPDAIMEAINASIGFDRRLARQDIDGSRAHAAMLAQQGILSSKD
AEAIREGLLTVLSEIETGQFAFSAALEDIHMNVEARLKELIGEPAGRLHTGRSRNDQVAT
DFKLWVRDQLDAADAGLLALLRALLAQAEAGADWVMPGFTHLQTAQPVTWGHHMMAYVEM
FARDRGRMQDARARMNECPLGAAALAGTSFPLDRDATAQALGFDRPAANSLDAVSDRDFA
LEFLAAASICAMHLSRMAEELVIWSSAQFRFVTLSDRFSTGSSIMPQKKNPDAAELIRAK
IGRIVGANVALLTVMKGLPLAYSKDMQEDKEQVFDAADTLMLALAAMEGMVRDMTANRAS
LEDAAASGFSTATDLADWLVRELNLPFRDAHHVTGTLVAMAEAKGCDLPDLSLAEMQSVH
GAIRADVFEVLGVHNSVASRTSYGGTAPSQVRAQVARWKERLG
Or try a new SitesBLAST search
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