SitesBLAST
Comparing WP_057687279.1 NCBI__GCF_001431535.1:WP_057687279.1 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
36% identity, 83% coverage: 28:386/431 of query aligns to 15:376/450 of 2e9fB
- active site: E71 (= E84), T146 (= T157), H147 (= H158), S268 (= S280), S269 (= S281), K274 (= K286), E281 (= E293)
- binding arginine: R98 (= R111), N99 (= N112), V102 (= V115), Y308 (= Y319), Q313 (= Q324), K316 (= K327)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
34% identity, 90% coverage: 12:397/431 of query aligns to 16:402/464 of P04424
- D31 (= D29) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ H49) mutation to N: 2-fold reduction in activity.
- K69 (≠ V67) 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 (≠ E176) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ I179) to S: in a breast cancer sample; somatic mutation
- R182 (≠ D180) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R184) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G198) to V: in a breast cancer sample; somatic mutation
- R236 (= R234) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (≠ K236) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (≠ N285) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R287) 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 (= R296) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A304) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q324) to L: in ARGINSA; severe
- V335 (≠ G333) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L358) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V380) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R383) to L: in ARGINSA; severe
- H388 (≠ Y386) to Q: in ARGINSA; severe
- A398 (= A393) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
Sites not aligning to the query:
- 12 R → Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- 456 R → 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)
34% identity, 84% coverage: 36:397/431 of query aligns to 40:404/468 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 (= T157) 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 (= H158) mutation to E: Loss of activity.
- R238 (≠ G235) mutation to Q: Loss of activity.
- T281 (= T278) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S280) 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 (= N288) binding in chain B; mutation to L: Loss of activity.
- D293 (= D290) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E293) mutation to D: Loss of activity.
- Y323 (= Y319) binding in chain A
- K325 (≠ R321) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q324) binding in chain A
- D330 (≠ S326) mutation to N: Loss of activity.
- K331 (= K327) 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)
34% identity, 84% coverage: 36:397/431 of query aligns to 23:387/450 of 1k7wD
- active site: E71 (= E84), T144 (= T157), H145 (= H158), A266 (≠ S280), S267 (= S281), K272 (= K286), E279 (= E293)
- binding argininosuccinate: R98 (= R111), N99 (= N112), V102 (= V115), T144 (= T157), H145 (= H158), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
33% identity, 87% coverage: 12:386/431 of query aligns to 5:379/451 of 1tj7B
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
33% identity, 84% coverage: 36:397/431 of query aligns to 21:385/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
31% identity, 84% coverage: 36:397/431 of query aligns to 38:402/466 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, 90% coverage: 35:420/431 of query aligns to 21:398/418 of 6ienC
- binding arginine: R98 (= R111), N99 (= N112), V102 (= V115), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
- binding argininosuccinate: T144 (= T157), H145 (= H158), S266 (= S280), S267 (= S281), M269 (= M283), K272 (= K286)
- binding fumaric acid: S97 (= S110), R98 (= R111), N99 (= N112)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
34% identity, 82% coverage: 35:387/431 of query aligns to 21:375/454 of 6ienB
- binding argininosuccinate: S97 (= S110), R98 (= R111), N99 (= N112), T144 (= T157), H145 (= H158), S266 (= S280), S267 (= S281), M269 (= M283), K272 (= K286), Y306 (= Y319), Q311 (= Q324), K314 (= K327)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
34% identity, 82% coverage: 35:387/431 of query aligns to 21:373/452 of 6ienA
- binding argininosuccinate: R98 (= R111), N99 (= N112), V102 (= V115), T144 (= T157), H145 (= H158), Y304 (= Y319), Q309 (= Q324), K312 (= K327)
- binding fumaric acid: S266 (= S280), S267 (= S281), K270 (= K286), N272 (= N288)
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
29% identity, 63% coverage: 26:296/431 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, 63% coverage: 26:296/431 of query aligns to 29:292/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
29% identity, 63% coverage: 26:296/431 of query aligns to 29:292/497 of 6g3fA
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
29% identity, 63% coverage: 26:296/431 of query aligns to 29:292/496 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)
22% identity, 75% coverage: 94:418/431 of query aligns to 77:411/431 of P12047
- H89 (= H106) mutation to Q: Abolishes enzyme activity.
- H141 (= H158) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ I228) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N288) mutation N->D,L: Abolishes enzyme activity.
- R301 (= R321) mutation R->K,Q: Abolishes enzyme activity.
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
26% identity, 45% coverage: 105:296/431 of query aligns to 132:331/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
26% identity, 45% coverage: 105:296/431 of query aligns to 131:330/462 of 3r6qA
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)
26% identity, 45% coverage: 98:293/431 of query aligns to 81:275/431 of Q9X0I0
- H141 (= H158) active site, Proton donor/acceptor
A0A0K2JL82 Nitrosuccinate lyase; EC 4.3.99.5 from Streptomyces cremeus (see paper)
29% identity, 48% coverage: 105:313/431 of query aligns to 117:335/476 of A0A0K2JL82
- D125 (= D113) mutation D->N,V: Almost loss of activity.
- R137 (≠ E125) binding
- R140 (≠ Q128) binding
- R201 (= R186) binding
- H253 (≠ Y229) mutation to A: Loss of activity.
- S302 (= S280) mutation to A: Loss of activity.
- K308 (= K286) binding ; mutation to A: Loss of activity.
- N310 (= N288) binding ; mutation to A: Loss of activity.
Sites not aligning to the query:
- 93 N→A: Slight decrease in activity.
- 341 R→A: Loss of activity.
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
21% identity, 73% coverage: 89:402/431 of query aligns to 71:387/427 of 2x75A
Sites not aligning to the query:
Query Sequence
>WP_057687279.1 NCBI__GCF_001431535.1:WP_057687279.1
MADLLWQKPGVAVDAKIQTFLAGDDVILDREFFLHDIAASAAHAEGLAHIGILSADELAG
LQRELEVLADDFRAGRFVLDEQYEDGHSAIEARLTDRLGDAGRRIHTGRSRNDQVLVATR
LWLKEKLQRVAQLSAEIAKVALDRADAEKDLPIPGYTHIQRAVVSSAGMWWAGWAEAFID
NAIRARDTHALVDANPLGTAAGYGVNLPLDREHTTAALGFARMQVSPIYAQLSRGKFEMA
ALEALGGATLDLRRIAWDLSLFTSAEFGFVALPAQYTTGSSIMPNKRNPDVIELMRATHA
SVAAARTEIEQLLSLPSGYHRDLQGSKGAIFHGFGRGLAALELLPALLANLEWRNDKLLA
GIDSGMYATDVAVEAAVAGVPFREAYKAAAAGADTAGQGRTPEGSLAARVSPGAAADLRL
DVLRARWQALA
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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