SitesBLAST
Comparing 352328 FitnessBrowser__Btheta:352328 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)
8wdqA Crystal structure of pseudomonas aeruginosa suhb in complex with d- myo-inositol-1-phosphate
36% identity, 94% coverage: 13:264/267 of query aligns to 12:265/273 of 8wdqA
- binding calcium ion: E69 (= E70), D88 (= D86), D88 (= D86), L90 (= L88), D91 (= D89), D91 (= D89), D218 (= D214)
- binding d-myo-inositol-1-phosphate: D91 (= D89), G92 (= G90), F163 (≠ Y161), R164 (vs. gap), R190 (≠ M186), G192 (= G188), A193 (≠ S189), A194 (= A190), E211 (= E207), D218 (= D214)
P0ADG4 Nus factor SuhB; Inositol-1-monophosphatase; I-1-Pase; IMPase; Inositol-1-phosphatase; EC 3.1.3.25 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 89% coverage: 12:248/267 of query aligns to 9:246/267 of P0ADG4
- E67 (= E70) binding Mg(2+)
- D84 (= D86) binding Mg(2+)
- L86 (= L88) binding Mg(2+)
- D87 (= D89) mutation to N: Loss of IMPase activity, still complements dnaB121 helicase mutation.
- R139 (≠ E141) mutation to C: In suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with A-250.
- G173 (≠ D175) mutation to V: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNA polymerase (RNAP).
- R183 (= R185) mutation to A: Some growth at 30 degrees Celsius, greater IMPase activity, partially inhibited by RNAP.
- R184 (≠ M186) mutation to A: Grows at 30 degrees Celsius, makes more dimer, partially inhibited by RNAP, crystallizes.; mutation to I: No growth at 30 degrees Celsius, IMPase activity not inhibited by RNAP.
Sites not aligning to the query:
- 250 V→A: In suhB10; decreases polypeptide chain elongation rate, grows at 30 but not 25 degrees Celsius; when associated with C-139.
- 251:254 KAML→AAMA: 3-fold decreased affinity for NusA, less efficient in delaying or suppressing Rho-dependent transcription termination.
2qflA Structure of suhb: inositol monophosphatase and extragenic suppressor from e. Coli (see paper)
34% identity, 89% coverage: 12:248/267 of query aligns to 9:246/262 of 2qflA
6ib8B Structure of a complex of suhb and nusa ar2 domain (see paper)
34% identity, 89% coverage: 12:248/267 of query aligns to 13:250/270 of 6ib8B
6tqoT Rrn anti-termination complex (see paper)
35% identity, 89% coverage: 12:248/267 of query aligns to 9:238/255 of 6tqoT
Q9M8S8 Inositol-phosphate phosphatase; L-galactose 1-phosphate phosphatase; Myo-inositol monophosphatase; EC 3.1.3.25; EC 3.1.3.93 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 88% coverage: 26:259/267 of query aligns to 26:266/271 of Q9M8S8
- P92 (= P87) mutation to L: In vtc4-1; low levels of ascorbate.
4as5A Structure of mouse inositol monophosphatase 1 (see paper)
32% identity, 94% coverage: 14:265/267 of query aligns to 13:269/274 of 4as5A
- active site: E68 (= E70), D88 (= D86), I90 (≠ L88), D91 (= D89), T93 (= T91), D218 (= D214)
- binding magnesium ion: E68 (= E70), D88 (= D86), D88 (= D86), I90 (≠ L88), D91 (= D89), D91 (= D89), D218 (= D214)
- binding phosphate ion: E68 (= E70), D88 (= D86), D91 (= D89), G92 (= G90)
3lv0A Crystal structure of extragenic suppressor protein suhb from bartonella henselae, native
33% identity, 91% coverage: 11:252/267 of query aligns to 7:247/258 of 3lv0A
O55023 Inositol monophosphatase 1; IMP 1; IMPase 1; D-galactose 1-phosphate phosphatase; Inositol-1(or 4)-monophosphatase 1; Lithium-sensitive myo-inositol monophosphatase A1; EC 3.1.3.25; EC 3.1.3.94 from Mus musculus (Mouse) (see paper)
31% identity, 94% coverage: 14:265/267 of query aligns to 15:271/277 of O55023
- E70 (= E70) binding Mg(2+)
- D90 (= D86) binding Mg(2+); binding Mg(2+)
- I92 (≠ L88) binding Mg(2+)
- D93 (= D89) binding Mg(2+)
- D220 (= D214) binding Mg(2+)
3luzA Crystal structure of extragenic suppressor protein suhb from bartonella henselae, via combined iodide sad molecular replacement (see paper)
34% identity, 82% coverage: 34:252/267 of query aligns to 18:229/238 of 3luzA
Sites not aligning to the query:
2hhmA Structure of inositol monophosphatase, the putative target of lithium therapy (see paper)
31% identity, 95% coverage: 14:266/267 of query aligns to 11:268/272 of 2hhmA
- active site: D43 (= D47), E66 (= E70), D86 (= D86), I88 (≠ L88), D89 (= D89), T91 (= T91), D216 (= D214)
- binding sulfate ion: E66 (= E70), D86 (= D86), D89 (= D89), G90 (= G90), T91 (= T91)
1imbA Structural analysis of inositol monophosphatase complexes with substrates (see paper)
31% identity, 95% coverage: 14:266/267 of query aligns to 11:268/272 of 1imbA
- active site: D43 (= D47), E66 (= E70), D86 (= D86), I88 (≠ L88), D89 (= D89), T91 (= T91), D216 (= D214)
- binding l-myo-inositol-1-phosphate: D89 (= D89), G90 (= G90), S161 (≠ Y163), T191 (≠ S189), A192 (= A190), E209 (= E207), D216 (= D214)
1awbA Human myo-inositol monophosphatase in complex with d-inositol-1- phosphate and calcium
31% identity, 95% coverage: 14:266/267 of query aligns to 11:268/272 of 1awbA
- active site: D43 (= D47), E66 (= E70), D86 (= D86), I88 (≠ L88), D89 (= D89), T91 (= T91), D216 (= D214)
- binding calcium ion: E66 (= E70), D86 (= D86), D86 (= D86), I88 (≠ L88), D89 (= D89), D216 (= D214)
- binding d-myo-inositol-1-phosphate: D86 (= D86), D89 (= D89), G90 (= G90), E158 (= E158), G190 (= G188), T191 (≠ S189), A192 (= A190), E209 (= E207)
P29218 Inositol monophosphatase 1; IMP 1; IMPase 1; D-galactose 1-phosphate phosphatase; Inositol-1(or 4)-monophosphatase 1; Lithium-sensitive myo-inositol monophosphatase A1; EC 3.1.3.25; EC 3.1.3.94 from Homo sapiens (Human) (see 5 papers)
31% identity, 94% coverage: 14:265/267 of query aligns to 15:271/277 of P29218
- K36 (≠ E36) mutation to Q: 50-fold reduction in activity.
- E70 (= E70) binding Mg(2+); binding substrate
- D90 (= D86) binding Mg(2+); binding Mg(2+)
- I92 (≠ L88) binding Mg(2+)
- IDGT 92:95 (≠ LDGT 88:91) binding substrate
- D93 (= D89) binding Mg(2+); mutation to N: Loss of activity.
- S165 (≠ Y163) mutation S->A,I: Reduced enzyme activity with myo-inositol 1-phosphate.
- GTA 194:196 (≠ GSA 188:190) binding substrate
- E213 (= E207) binding substrate; mutation to Q: Strongly reduced affinity for myo-inositol 1-phosphate and strongly reduced enzyme activity with myo-inositol 1-phosphate.
- D220 (= D214) binding Mg(2+); binding substrate
6zk0AAA human impase with ebselen (see paper)
31% identity, 95% coverage: 14:266/267 of query aligns to 12:269/274 of 6zk0AAA
4as4A Structure of human inositol monophosphatase 1 (see paper)
31% identity, 95% coverage: 14:266/267 of query aligns to 13:270/274 of 4as4A
- active site: D45 (= D47), E68 (= E70), D88 (= D86), I90 (≠ L88), D91 (= D89), T93 (= T91), D218 (= D214)
- binding magnesium ion: E68 (= E70), D88 (= D86), D88 (= D86), I90 (≠ L88), D91 (= D89), D218 (= D214)
- binding phosphate ion: E68 (= E70), D88 (= D86), I90 (≠ L88), D91 (= D89), G92 (= G90), T93 (= T91)
6giuA Human impase with l-690330 (see paper)
31% identity, 94% coverage: 14:265/267 of query aligns to 13:269/275 of 6giuA
- active site: E68 (= E70), D88 (= D86), I90 (≠ L88), D91 (= D89), T93 (= T91), D218 (= D214)
- binding [1-(4-oxidanylphenoxy)-1-phosphono-ethyl]phosphonic acid: E68 (= E70), D88 (= D86), D91 (= D89), G92 (= G90), T93 (= T91), E160 (= E158), G192 (= G188), A194 (= A190), E211 (= E207), W217 (= W213), D218 (= D214)
- binding manganese (ii) ion: E68 (= E70), D88 (= D86), D88 (= D86), I90 (≠ L88), D91 (= D89), D91 (= D89), D218 (= D214)
1imdA Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis (see paper)
32% identity, 89% coverage: 14:251/267 of query aligns to 11:253/266 of 1imdA