SitesBLAST
Comparing Pf1N1B4_2183 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2183 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
53% identity, 94% coverage: 19:452/464 of query aligns to 3:438/450 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)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
50% identity, 97% coverage: 13:461/464 of query aligns to 1:450/451 of 1tj7B
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, 97% coverage: 10:461/464 of query aligns to 11:461/468 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.
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 99% coverage: 5:464/464 of query aligns to 4:462/464 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 (= K52) 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 (≠ S182) 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 (= M361) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ L384) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R387) to L: in ARGINSA; severe
- H388 (= H390) to Q: in ARGINSA; severe
- A398 (≠ G400) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (≠ Q458) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
43% identity, 95% coverage: 19:461/464 of query aligns to 3:444/450 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)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
41% identity, 95% coverage: 19:461/464 of query aligns to 1:442/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
40% identity, 97% coverage: 10:461/464 of query aligns to 9:459/466 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)
44% identity, 94% coverage: 17:452/464 of query aligns to 1:436/454 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)
44% identity, 94% coverage: 17:452/464 of query aligns to 1:434/452 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)
42% identity, 94% coverage: 17:452/464 of query aligns to 1:400/418 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)
33% identity, 83% coverage: 27:413/464 of query aligns to 27:405/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
33% identity, 83% coverage: 27:413/464 of query aligns to 27:405/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
33% identity, 83% coverage: 27:413/464 of query aligns to 27:405/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
33% identity, 83% coverage: 27:413/464 of query aligns to 27:405/496 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, 65% coverage: 108:410/464 of query aligns to 132:450/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
26% identity, 65% coverage: 108:410/464 of query aligns to 131:449/462 of 3r6qA
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, 55% coverage: 97:351/464 of query aligns to 77:331/431 of P12047
- H89 (= H109) mutation to Q: Abolishes enzyme activity.
- H141 (= H161) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ N233) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N290) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K324) mutation R->K,Q: Abolishes enzyme activity.
6wngA Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis nuhp1
25% identity, 66% coverage: 108:413/464 of query aligns to 135:441/466 of 6wngA
Sites not aligning to the query:
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 50% coverage: 96:325/464 of query aligns to 75:301/427 of 2x75A
Sites not aligning to the query:
P9WN93 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
28% identity, 33% coverage: 155:306/464 of query aligns to 181:342/474 of P9WN93
- T186 (= T160) binding
- S318 (= S282) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S283) binding
- KVN 324:326 (≠ KKN 288:290) binding
Sites not aligning to the query:
- 104:106 binding
- 138:140 binding
Query Sequence
>Pf1N1B4_2183 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2183
MSTDKTNQSWGGRFSEPVDAFVARFTASVTFDQRLYRHDIMGSIAHASMLAKVGVLTDAE
RDSIIDGLNTIQGEIEAGQFDWRIDLEDVHMNIEARLTDRIGVTGKKLHTGRSRNDQVAT
DIRLWLRDEIDLILGEITRLQQGLLEQAEREAASIMPGFTHLQTAQPVTFGHHMLAWFEM
LSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDREYTAQLLGFDAVGGNSLDNVSDRDFA
IEFCSAASIAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGK
TGRVFGALMGLLTLMKGQPLAYNKDNQEDKEPLFDAADTLRDSLRAFADMIPAIKPKHAM
MREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTGKDLAEMSLEELRKFSD
QIEQDVFAVLTLEGSVNARDHIGGTAPAQVKKAVARGQALLASR
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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