SitesBLAST
Comparing WP_011992986.1 NCBI__GCF_000017645.1:WP_011992986.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
35% identity, 75% coverage: 89:467/505 of query aligns to 69:442/450 of 2e9fB
- active site: E71 (≠ G91), T146 (= T163), H147 (≠ Y164), S268 (= S285), S269 (≠ K286), K274 (= K291), E281 (≠ A298)
- binding arginine: R98 (= R117), N99 (≠ R118), V102 (≠ L121), Y308 (≠ Q324), Q313 (≠ A331), K316 (≠ A334)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
30% identity, 73% coverage: 92:461/505 of query aligns to 77:439/451 of 1tj7B
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
28% identity, 76% coverage: 92:477/505 of query aligns to 70:447/447 of 1hy0A
Sites not aligning to the query:
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
28% identity, 76% coverage: 92:477/505 of query aligns to 72:449/450 of 1k7wD
- active site: T144 (= T163), H145 (≠ Y164), A266 (≠ S285), S267 (≠ K286), K272 (= K291), E279 (≠ A298)
- binding argininosuccinate: R98 (= R117), N99 (≠ R118), V102 (≠ L121), T144 (= T163), H145 (≠ Y164), Y306 (≠ Q324), Q311 (≠ M329), K314 (≠ Y332)
Sites not aligning to the query:
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)
28% identity, 76% coverage: 92:477/505 of query aligns to 89:466/468 of P24058
- D89 (= D92) mutation to N: Loss of activity.
- N116 (≠ R118) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (≠ E119) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T163) 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 (≠ Y164) mutation to E: Loss of activity.
- R238 (≠ A240) mutation to Q: Loss of activity.
- T281 (≠ R283) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S285) 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 (= N293) binding in chain B; mutation to L: Loss of activity.
- D293 (≠ Y295) mutation to N: 99% decrease in catalytic efficiency.
- E296 (≠ A298) mutation to D: Loss of activity.
- Y323 (≠ Q324) binding in chain A
- K325 (≠ D326) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ M329) binding in chain A
- D330 (≠ A331) mutation to N: Loss of activity.
- K331 (≠ Y332) 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.
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
27% identity, 92% coverage: 15:477/505 of query aligns to 9:464/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
29% identity, 90% coverage: 16:468/505 of query aligns to 10:455/464 of P04424
- R12 (= R18) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (≠ S43) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (vs. gap) mutation to N: 2-fold reduction in activity.
- K69 (≠ L78) modified: N6-acetyllysine
- E73 (≠ G82) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D92) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (≠ Y94) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A99) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R100) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R117) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ A124) to E: in ARGINSA; severe
- V178 (≠ W182) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L185) to S: in a breast cancer sample; somatic mutation
- R182 (= R186) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R190) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G204) to V: in a breast cancer sample; somatic mutation
- R236 (≠ A240) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D241) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q290) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (≠ R292) 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 (= R301) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ A310) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (≠ M329) to L: in ARGINSA; severe
- V335 (≠ A338) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (vs. gap) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ L387) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R390) to L: in ARGINSA; severe
- H388 (= H393) to Q: in ARGINSA; severe
- A398 (≠ L403) 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
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
35% identity, 70% coverage: 109:464/505 of query aligns to 90:437/454 of 6ienB
- binding argininosuccinate: S97 (≠ A116), R98 (= R117), N99 (≠ R118), T144 (= T163), H145 (≠ Y164), S266 (= S285), S267 (≠ K286), M269 (≠ L288), K272 (= K291), Y306 (≠ Q324), Q311 (≠ A331), K314 (≠ A334)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
36% identity, 59% coverage: 109:405/505 of query aligns to 90:382/418 of 6ienC
- binding arginine: R98 (= R117), N99 (≠ R118), V102 (≠ L121), Y306 (≠ Q324), Q311 (≠ A331), K314 (≠ A334)
- binding argininosuccinate: T144 (= T163), H145 (≠ Y164), S266 (= S285), S267 (≠ K286), M269 (≠ L288), K272 (= K291)
- binding fumaric acid: S97 (≠ A116), R98 (= R117), N99 (≠ R118)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
34% identity, 70% coverage: 109:464/505 of query aligns to 90:435/452 of 6ienA
- binding argininosuccinate: R98 (= R117), N99 (≠ R118), V102 (≠ L121), T144 (= T163), H145 (≠ Y164), Y304 (≠ Q324), Q309 (≠ A331), K312 (≠ A334)
- binding fumaric acid: S266 (= S285), S267 (≠ K286), K270 (= K291), N272 (= N293)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
27% identity, 83% coverage: 44:462/505 of query aligns to 37:451/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
27% identity, 83% coverage: 44:462/505 of query aligns to 37:451/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
27% identity, 83% coverage: 44:462/505 of query aligns to 37:451/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
27% identity, 83% coverage: 44:462/505 of query aligns to 37:451/497 of 6g3fA
Query Sequence
>WP_011992986.1 NCBI__GCF_000017645.1:WP_011992986.1
MTRLSDRSAGAVLEIGNRLSAAPSPRMVAVAFAEEVSGQVPLSPHLVLVDLAHVITLAER
DVIPRGPARDLVGALLDLHDEGGAEALAELGDLYTNHEARIAARTAAAGWLGTARARREA
LTTAYHLLLRERLLVLGTALTRLGRRLAAAALAHADQVMPDYTYLQAAQPTSLGHYLLGF
AWPVLRDLGRLEALYVRTDLCPAGCGSMNGSVAFQDRAALSRRLGFSSPLAHGRDAMWQA
DLAIEAMALSVTASVGLDRLAEDLMIFATAEFGLVRLADKHSRASKILPQKRNPYALAFI
RGLANRLIGAQAGVAASARTPTGQMDNRMLAYGAVPEALGSCAEATDLMAEIIGALSFDG
ARAEALLADGACFASDLAERLCLALGLDFRRAHGLVGRLVTRLEGEERALSTLTQDELSA
ACHAFDAALPPVPDGLLAAAFDPKTCLEARRDVGGAAPQEVRRQARELDDTFRHRAEDLA
ATARRNAMALGSLVGEARSCSGRAP
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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