SitesBLAST
Comparing SM_b21094 FitnessBrowser__Smeli:SM_b21094 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)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
53% identity, 90% coverage: 16:452/488 of query aligns to 1:438/454 of 6ienB
- binding argininosuccinate: S97 (= S111), R98 (= R112), N99 (= N113), T144 (= T158), H145 (= H159), S266 (= S280), S267 (= S281), M269 (= M283), K272 (= K286), Y306 (= Y320), Q311 (≠ A325), K314 (= K328)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
53% identity, 90% coverage: 16:452/488 of query aligns to 1:436/452 of 6ienA
- binding argininosuccinate: R98 (= R112), N99 (= N113), V102 (≠ T116), T144 (= T158), H145 (= H159), Y304 (= Y320), Q309 (≠ A325), K312 (= K328)
- binding fumaric acid: S266 (= S280), S267 (= S281), K270 (= K286), N272 (= N288)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
54% identity, 82% coverage: 16:416/488 of query aligns to 1:405/418 of 6ienC
- binding arginine: R98 (= R112), N99 (= N113), V102 (≠ T116), Y306 (= Y320), Q311 (≠ A325), K314 (= K328)
- binding argininosuccinate: T144 (= T158), H145 (= H159), S266 (= S280), S267 (= S281), M269 (= M283), K272 (= K286)
- binding fumaric acid: S97 (= S111), R98 (= R112), N99 (= N113)
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
42% identity, 90% coverage: 15:452/488 of query aligns to 1:440/450 of 2e9fB
- active site: E71 (= E85), T146 (= T158), H147 (= H159), S268 (= S280), S269 (= S281), K274 (= K286), E281 (= E293)
- binding arginine: R98 (= R112), N99 (= N113), V102 (≠ T116), Y308 (= Y320), Q313 (≠ A325), K316 (= K328)
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)
35% identity, 92% coverage: 6:455/488 of query aligns to 9:457/468 of P24058
- W11 (= W8) 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 (≠ A26) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (≠ Y30) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D86) mutation to N: Loss of activity.
- N116 (= N113) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D114) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T158) 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 (= H159) mutation to E: Loss of activity.
- R238 (= R235) 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 (= Y320) binding in chain A
- K325 (≠ R322) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (≠ A325) binding in chain A
- D330 (= D327) mutation to N: Loss of activity.
- K331 (= K328) 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)
37% identity, 92% coverage: 2:452/488 of query aligns to 3:452/464 of P04424
- R12 (= R11) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (≠ F31) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ R50) mutation to N: 2-fold reduction in activity.
- K69 (≠ G68) modified: N6-acetyllysine
- E73 (≠ D72) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D86) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H88) mutation to Q: 10-fold reduction in activity.
- R94 (= R93) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ L94) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R112) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ N119) to E: in ARGINSA; severe
- V178 (≠ Q177) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L180) to S: in a breast cancer sample; somatic mutation
- R182 (= R181) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R185) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G199) to V: in a breast cancer sample; somatic mutation
- R236 (= R235) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D236) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q285) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K287) 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 (≠ N305) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (≠ A325) to L: in ARGINSA; severe
- V335 (≠ T334) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (≠ L359) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V382) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (≠ A385) to L: in ARGINSA; severe
- H388 (= H388) to Q: in ARGINSA; severe
- A398 (≠ C398) 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
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
36% identity, 87% coverage: 32:455/488 of query aligns to 18:440/450 of 1k7wD
- active site: E71 (= E85), T144 (= T158), H145 (= H159), A266 (≠ S280), S267 (= S281), K272 (= K286), E279 (= E293)
- binding argininosuccinate: R98 (= R112), N99 (= N113), V102 (≠ T116), T144 (= T158), H145 (= H159), Y306 (= Y320), Q311 (≠ A325), K314 (= K328)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
35% identity, 89% coverage: 23:455/488 of query aligns to 7:438/447 of 1hy0A
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
37% identity, 91% coverage: 11:453/488 of query aligns to 1:444/451 of 1tj7B
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
34% identity, 93% coverage: 2:455/488 of query aligns to 3:455/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
36% identity, 74% coverage: 42:402/488 of query aligns to 44:396/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
36% identity, 74% coverage: 42:402/488 of query aligns to 44:396/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
36% identity, 74% coverage: 42:402/488 of query aligns to 44:396/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
36% identity, 74% coverage: 42:402/488 of query aligns to 44:396/497 of 6g3fA
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
23% identity, 65% coverage: 106:422/488 of query aligns to 131:458/462 of 3r6qA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
23% identity, 65% coverage: 106:422/488 of query aligns to 132:459/463 of 3r6vG
4adlA Crystal structures of rv1098c in complex with malate (see paper)
27% identity, 48% coverage: 138:371/488 of query aligns to 158:402/459 of 4adlA
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)
27% identity, 48% coverage: 138:371/488 of query aligns to 166:410/474 of P9WN93
- T186 (= T158) binding
- S318 (= S280) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S281) binding
- KVN 324:326 (≠ KKN 286:288) binding
Sites not aligning to the query:
- 104:106 binding
- 138:140 binding
6wngA Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis nuhp1
24% identity, 41% coverage: 106:305/488 of query aligns to 135:343/466 of 6wngA
Sites not aligning to the query:
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
27% identity, 48% coverage: 138:371/488 of query aligns to 158:402/462 of 4apbD
Sites not aligning to the query:
Query Sequence
>SM_b21094 FitnessBrowser__Smeli:SM_b21094
MTEPTQLWGGRFKSGPSEALANLSRAPRSYFRLYKEDIAGSRAHASELKRAGVLDESEFS
AIRAALEGIEADVGAGREEPIAADEDLHTFLERLLMARLGTLGGKLRAGRSRNDQTANNT
RLYLRRMARELSQGVIAIEEALTEQASRHTETVMPGFTHLQPAQPVVLGHHLMAHAQSLL
RDLQRFADWDRRFDRSPLGAAALAGSGIARRPDLSAIDLGYSAACENSIDAVAARDHVAE
FLFICSLVAVDLSRLAEEICLWSSKQFSWVRLHDSYSTGSSIMPQKKNPDVAELTRGMSG
TLIGNIAGFLATMKAMPLAYNRDLAEDKRSLFETIDVLELVLPAFAGMVGTLEFDVEKLR
EEAPKGFTLATEVADWLVGRDVPFAEAHEITGAVVRFCEERGHDLAGLTAEDLPGIDPRL
HPEMLAALVLEKALASRNGYGATAPEKVREQIARFETALAECCAFAGGPIGGGAFAGAKD
GAEEARRR
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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