SitesBLAST
Comparing GFF244 FitnessBrowser__Marino:GFF244 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
51% identity, 95% coverage: 26:469/469 of query aligns to 3:448/450 of 2e9fB
- active site: E71 (= E94), T146 (= T167), H147 (= H168), S268 (= S289), S269 (= S290), K274 (= K295), E281 (= E302)
- binding arginine: R98 (= R121), N99 (= N122), V102 (= V125), Y308 (= Y329), Q313 (= Q334), K316 (= K337)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
49% identity, 96% coverage: 20:469/469 of query aligns to 1:451/451 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)
45% identity, 96% coverage: 14:465/469 of query aligns to 8:458/468 of P24058
- W11 (= W17) 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 (= S35) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D39) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D95) mutation to N: Loss of activity.
- N116 (= N122) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D123) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T167) 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 (= H168) mutation to E: Loss of activity.
- R238 (= R244) mutation to Q: Loss of activity.
- T281 (= T287) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S289) 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 (= N297) binding in chain B; mutation to L: Loss of activity.
- D293 (= D299) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E302) mutation to D: Loss of activity.
- Y323 (= Y329) binding in chain A
- K325 (= K331) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q334) binding in chain A
- D330 (= D336) mutation to N: Loss of activity.
- K331 (= K337) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 94% coverage: 25:465/469 of query aligns to 2:441/450 of 1k7wD
- active site: E71 (= E94), T144 (= T167), H145 (= H168), A266 (≠ S289), S267 (= S290), K272 (= K295), E279 (= E302)
- binding argininosuccinate: R98 (= R121), N99 (= N122), V102 (= V125), T144 (= T167), H145 (= H168), Y306 (= Y329), Q311 (= Q334), K314 (= K337)
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 98% coverage: 11:468/469 of query aligns to 3:459/464 of P04424
- R12 (= R20) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D39) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ E59) mutation to N: 2-fold reduction in activity.
- K69 (≠ G77) modified: N6-acetyllysine
- E73 (≠ D81) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D95) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H97) mutation to Q: 10-fold reduction in activity.
- R94 (≠ A102) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (= R103) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R121) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (= D128) to E: in ARGINSA; severe
- V178 (≠ E186) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ V189) to S: in a breast cancer sample; somatic mutation
- R182 (= R190) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R194) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G208) to V: in a breast cancer sample; somatic mutation
- R236 (= R244) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D245) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q294) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K296) 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 (= R305) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ H314) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q334) to L: in ARGINSA; severe
- V335 (≠ T343) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M368) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V391) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R394) to L: in ARGINSA; severe
- H388 (= H397) to Q: in ARGINSA; severe
- A398 (≠ G407) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R465) to 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)
42% identity, 94% coverage: 26:465/469 of query aligns to 1:439/447 of 1hy0A
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 98% coverage: 11:468/469 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)
44% identity, 95% coverage: 24:468/469 of query aligns to 1:448/454 of 6ienB
- binding argininosuccinate: S97 (= S120), R98 (= R121), N99 (= N122), T144 (= T167), H145 (= H168), S266 (= S289), S267 (= S290), M269 (= M292), K272 (= K295), Y306 (= Y329), Q311 (= Q334), K314 (= K337)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 95% coverage: 24:468/469 of query aligns to 1:446/452 of 6ienA
- binding argininosuccinate: R98 (= R121), N99 (= N122), V102 (= V125), T144 (= T167), H145 (= H168), Y304 (= Y329), Q309 (= Q334), K312 (= K337)
- binding fumaric acid: S266 (= S289), S267 (= S290), K270 (= K295), N272 (= N297)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 95% coverage: 24:468/469 of query aligns to 1:412/418 of 6ienC
- binding arginine: R98 (= R121), N99 (= N122), V102 (= V125), Y306 (= Y329), Q311 (= Q334), K314 (= K337)
- binding argininosuccinate: T144 (= T167), H145 (= H168), S266 (= S289), S267 (= S290), M269 (= M292), K272 (= K295)
- binding fumaric acid: S97 (= S120), R98 (= R121), N99 (= N122)
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
33% identity, 89% coverage: 52:468/469 of query aligns to 45:461/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
33% identity, 89% coverage: 52:468/469 of query aligns to 45:461/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
33% identity, 89% coverage: 52:468/469 of query aligns to 45:461/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
33% identity, 89% coverage: 52:468/469 of query aligns to 45:461/497 of 6g3fA
2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
24% identity, 64% coverage: 103:400/469 of query aligns to 75:374/427 of 2x75A
Sites not aligning to the query:
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
29% identity, 43% coverage: 115:314/469 of query aligns to 132:340/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
29% identity, 43% coverage: 115:314/469 of query aligns to 131:339/462 of 3r6qA
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)
23% identity, 57% coverage: 104:369/469 of query aligns to 77:342/431 of P12047
- H89 (= H116) mutation to Q: Abolishes enzyme activity.
- H141 (= H168) mutation to Q: Abolishes enzyme activity.
- Q212 (≠ S240) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
- N270 (= N297) mutation N->D,L: Abolishes enzyme activity.
- R301 (≠ K331) mutation R->K,Q: Abolishes enzyme activity.
3oceA Crystal structure of fumarate lyase:delta crystallin from brucella melitensis bound to cobalt
25% identity, 65% coverage: 115:419/469 of query aligns to 134:450/461 of 3oceA
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)
23% identity, 63% coverage: 108:403/469 of query aligns to 81:378/431 of Q9X0I0
- H141 (= H168) active site, Proton donor/acceptor
Query Sequence
>GFF244 FitnessBrowser__Marino:GFF244
MTDQKKSDQTTSSEKPWGGRFSEPTDAFVEKFTASVGFDQRLYHHDITGSIAHATMLAEV
GVLTTDERDQIIEGLKGVKADIEAGNFQWSVSLEDVHMNIEARLTDRIGITGKKLHTGRS
RNDQVATDIRLYLRDEIDVIAEELKRLQTGLLDLAEREADTIMPGFTHLQTAQPVTFGHH
LLAWYEMLVRDAERLQDCRKRVNVMPLGAAALAGTTYPIDRAMTARLLGFDRPTENSLDS
VSDRDFAIEFCSFAALLMTHLSRFSEELVLWTSAQFDFIDLPDRFCTGSSIMPQKKNPDV
PELVRGKTGRVNGHLISLLTLMKSQPLAYNKDNQEDKEPLFDTVDTIKGCLKAYADMIPA
IRSKADNMRVAAKRGFSTATDLADYLVKKGVPFRDAHEIVGKSVAFGVAEGRDLSDMTLE
ELQQFSDHIGADVFHVLTLEGSVQARDHLGGTAPDQVRAAVGRARNQLG
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