SitesBLAST
Comparing GFF2574 FitnessBrowser__Marino:GFF2574 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)
O53289 Phosphoserine phosphatase SerB2; PSP; PSPase; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; EC 3.1.3.3; EC 3.1.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
38% identity, 99% coverage: 5:409/410 of query aligns to 7:395/409 of O53289
- G18 (= G16) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- G108 (≠ E110) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- D185 (= D195) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M196) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D197) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S198) mutation to A: No effect on enzymatic activity.
- S273 (= S283) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K328) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D351) mutation to G: Decreases enzymatic activity by 80%.; mutation to N: Decreases enzymatic activity by 85%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-345.
- D345 (= D355) mutation to N: Decreases enzymatic activity by 55%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-341.
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
38% identity, 99% coverage: 5:409/410 of query aligns to 5:393/396 of 8a21A
- binding magnesium ion: D183 (= D195), D185 (= D197), D339 (= D351)
- binding 4-phenyl-1h-imidazole: D13 (= D13), T18 (= T18), Q37 (= Q37), D185 (= D197), E192 (= E204), V193 (= V205), I194 (= I206), T211 (= T223), M215 (= M227), F221 (= F233), R228 (= R240), G273 (= G285)
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
38% identity, 99% coverage: 5:409/410 of query aligns to 5:393/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D197), E192 (= E204), M215 (= M227), F221 (= F233), L225 (≠ F237), R228 (= R240), G272 (= G284), F274 (= F286), D339 (= D351)
- binding magnesium ion: D183 (= D195), D185 (= D197), D339 (= D351)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
38% identity, 99% coverage: 5:409/410 of query aligns to 5:393/396 of 5jlpA
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
37% identity, 99% coverage: 5:409/410 of query aligns to 9:397/411 of A0QJI1
- D187 (= D195) binding
- D189 (= D197) binding
- D343 (= D351) binding
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
46% identity, 51% coverage: 187:394/410 of query aligns to 1:208/209 of 1l7nA
- active site: D9 (= D195), F10 (≠ M196), D11 (= D197), G98 (= G284), K142 (= K328), D169 (= D355)
- binding aluminum fluoride: D9 (= D195), F10 (≠ M196), D11 (= D197), S97 (= S283), K142 (= K328)
- binding tetrafluoroaluminate ion: D9 (= D195), F10 (≠ M196), D11 (= D197), S97 (= S283), G98 (= G284), K142 (= K328), N168 (= N354)
- binding magnesium ion: D9 (= D195), D11 (= D197), D165 (= D351)
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
46% identity, 51% coverage: 187:394/410 of query aligns to 2:209/210 of 1f5sA
- active site: D10 (= D195), F11 (≠ M196), D12 (= D197), G99 (= G284), K143 (= K328), D170 (= D355)
- binding magnesium ion: D10 (= D195), D12 (= D197), D166 (= D351)
- binding phosphate ion: D10 (= D195), F11 (≠ M196), D12 (= D197), S98 (= S283), G99 (= G284), K143 (= K328)
Q58989 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see 3 papers)
46% identity, 51% coverage: 187:394/410 of query aligns to 3:210/211 of Q58989
- D11 (= D195) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D197) active site, Proton donor; binding
- E20 (= E204) binding
- R56 (= R240) binding
- SG 99:100 (= SG 283:284) binding
- K144 (= K328) binding
- D167 (= D351) binding
- N170 (= N354) binding
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
46% identity, 50% coverage: 189:394/410 of query aligns to 2:207/208 of 1l7pA
- active site: N8 (≠ D195), F9 (≠ M196), D10 (= D197), G97 (= G284), K141 (= K328), D168 (= D355)
- binding phosphoserine: N8 (≠ D195), F9 (≠ M196), D10 (= D197), E17 (= E204), M40 (= M227), F46 (= F233), R53 (= R240), S96 (= S283), G97 (= G284), K141 (= K328)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
44% identity, 56% coverage: 175:403/410 of query aligns to 68:295/295 of 7qplA
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
44% identity, 50% coverage: 189:394/410 of query aligns to 2:199/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 50% coverage: 189:394/410 of query aligns to 3:207/208 of 3m1yC
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
33% identity, 47% coverage: 192:383/410 of query aligns to 13:210/217 of 6q6jB
- binding calcium ion: D16 (= D195), D18 (= D197), D175 (= D351)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D195), V17 (≠ M196), D18 (= D197), F54 (= F233), S105 (= S283), G106 (= G284), G107 (= G285), K154 (= K328), T178 (≠ N354)
6hyjB Psph human phosphoserine phosphatase (see paper)
33% identity, 47% coverage: 192:383/410 of query aligns to 17:214/223 of 6hyjB
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 47% coverage: 192:383/410 of query aligns to 14:211/222 of 1l8oA
- active site: D17 (= D195), V18 (≠ M196), D19 (= D197), G107 (= G284), K155 (= K328), D180 (= D355)
- binding phosphate ion: D17 (= D195), D19 (= D197), S106 (= S283), K155 (= K328)
- binding serine: G177 (= G352), T179 (≠ N354), R199 (vs. gap)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 47% coverage: 192:383/410 of query aligns to 14:211/222 of 1l8lA
- active site: D17 (= D195), V18 (≠ M196), D19 (= D197), G107 (= G284), K155 (= K328), D180 (= D355)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D195), D19 (= D197), G107 (= G284), K155 (= K328), D176 (= D351), G177 (= G352), T179 (≠ N354)
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
33% identity, 47% coverage: 192:383/410 of query aligns to 13:210/221 of 6hyyA
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
33% identity, 47% coverage: 192:383/410 of query aligns to 17:214/225 of P78330
- D20 (= D195) binding
- DVD 20:22 (≠ DMD 195:197) binding
- D22 (= D197) binding
- S23 (= S198) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E204) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D207) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A210) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M227) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ Q228) binding
- R65 (= R240) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 283:285) binding ; binding
- N133 (= N305) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K328) binding ; binding
- D179 (= D351) binding
- T182 (≠ N354) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
- R202 (vs. gap) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
27% identity, 44% coverage: 189:367/410 of query aligns to 9:174/200 of 4ap9A
- active site: D15 (= D195), I16 (≠ M196), E17 (≠ D197), G103 (= G284), K141 (= K328), D162 (= D355)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ A211), I32 (≠ E212), T33 (≠ A213), L46 (≠ M227), W52 (≠ F233), D140 (= D324), K141 (= K328), Y160 (≠ A353), A161 (≠ N354)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
30% identity, 40% coverage: 192:356/410 of query aligns to 17:180/585 of 6iuyA
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532
Query Sequence
>GFF2574 FitnessBrowser__Marino:GFF2574
MSELVLINVSGRDKPGLTSEITGIMGRYDVRILDIGQAVIHDHLTWGILIEIPDESKSSP
VIRDLLFRLHALDLQVRFAPITVEEYQSWAAARNRACYIVTLLARDIKAEQIARVSAITA
RHGLNIDNISRLSARPSLNAADNRIACVEFSVRGTPSDLEKLRADFLHIAGEMNVDIAFQ
EDSIFRRNRRLVVFDMDSTLIEAEVIDELAAEAGVGEQVAEITERAMQGELDFSQSFAER
LALLKGLDESVLEGIASRLRMTEGAEHLILSLKALGYRTAILSGGFTYFARHLQRKLGID
YIYANELEIEGGKVTGKVSGQIVDGKRKAELLLEIAEKEHISREQVIAVGDGANDLPMLS
QAGLGVAFRAKPLVKESARHAISTLGLDAILYLIGFRESETNQSLENADF
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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