SitesBLAST
Comparing Dsui_2379 FitnessBrowser__PS:Dsui_2379 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)
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)
49% identity, 76% coverage: 66:278/280 of query aligns to 166:384/409 of O53289
- D185 (= D78) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M79) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D80) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S81) mutation to A: No effect on enzymatic activity.
- S273 (= S167) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K212) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D235) 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 (= D239) 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.
Sites not aligning to the query:
- 18 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- 108 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
47% identity, 73% coverage: 74:278/280 of query aligns to 183:386/411 of A0QJI1
- D187 (= D78) binding
- D189 (= D80) binding
- D343 (= D235) binding
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
47% identity, 73% coverage: 74:278/280 of query aligns to 179:382/396 of 8a21A
- binding magnesium ion: D183 (= D78), D185 (= D80), D339 (= D235)
- binding 4-phenyl-1h-imidazole: D185 (= D80), E192 (= E87), V193 (≠ C88), I194 (= I89), T211 (= T106), M215 (= M110), F221 (≠ Y116), R228 (= R123), G273 (= G169)
Sites not aligning to the query:
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
47% identity, 73% coverage: 74:278/280 of query aligns to 179:382/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D80), E192 (= E87), M215 (= M110), F221 (≠ Y116), L225 (= L120), R228 (= R123), G272 (= G168), F274 (= F170), D339 (= D235)
- binding magnesium ion: D183 (= D78), D185 (= D80), D339 (= D235)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
47% identity, 73% coverage: 74:278/280 of query aligns to 179:382/396 of 5jlpA
Sites not aligning to the query:
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
45% identity, 73% coverage: 74:277/280 of query aligns to 82:285/295 of 7qplA
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
39% identity, 72% coverage: 74:275/280 of query aligns to 5:205/209 of 1l7nA
- active site: D9 (= D78), F10 (≠ M79), D11 (= D80), G98 (= G168), K142 (= K212), D169 (= D239)
- binding aluminum fluoride: D9 (= D78), F10 (≠ M79), D11 (= D80), S97 (= S167), K142 (= K212)
- binding tetrafluoroaluminate ion: D9 (= D78), F10 (≠ M79), D11 (= D80), S97 (= S167), G98 (= G168), K142 (= K212), N168 (= N238)
- binding magnesium ion: D9 (= D78), D11 (= D80), D165 (= D235)
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
39% identity, 72% coverage: 74:275/280 of query aligns to 6:206/210 of 1f5sA
- active site: D10 (= D78), F11 (≠ M79), D12 (= D80), G99 (= G168), K143 (= K212), D170 (= D239)
- binding magnesium ion: D10 (= D78), D12 (= D80), D166 (= D235)
- binding phosphate ion: D10 (= D78), F11 (≠ M79), D12 (= D80), S98 (= S167), G99 (= G168), K143 (= K212)
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)
39% identity, 72% coverage: 74:275/280 of query aligns to 7:207/211 of Q58989
- D11 (= D78) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D80) active site, Proton donor; binding
- E20 (= E87) binding
- R56 (= R123) binding
- SG 99:100 (= SG 167:168) binding
- K144 (= K212) binding
- D167 (= D235) binding
- N170 (= N238) binding
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
39% identity, 72% coverage: 74:275/280 of query aligns to 4:204/208 of 1l7pA
- active site: N8 (≠ D78), F9 (≠ M79), D10 (= D80), G97 (= G168), K141 (= K212), D168 (= D239)
- binding phosphoserine: N8 (≠ D78), F9 (≠ M79), D10 (= D80), E17 (= E87), M40 (= M110), F46 (≠ Y116), R53 (= R123), S96 (= S167), G97 (= G168), K141 (= K212)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
37% identity, 72% coverage: 74:275/280 of query aligns to 4:196/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
36% identity, 69% coverage: 74:267/280 of query aligns to 5:196/208 of 3m1yC
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
28% identity, 64% coverage: 75:252/280 of query aligns to 13:192/221 of 6hyyA
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
28% identity, 64% coverage: 75:252/280 of query aligns to 13:192/217 of 6q6jB
- binding calcium ion: D16 (= D78), D18 (= D80), D175 (= D235)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D78), V17 (≠ M79), D18 (= D80), F54 (≠ Y116), S105 (= S167), G106 (= G168), G107 (= G169), K154 (= K212), T178 (≠ N238)
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
28% identity, 64% coverage: 75:252/280 of query aligns to 14:193/222 of 1l8oA
Sites not aligning to the query:
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
28% identity, 64% coverage: 75:252/280 of query aligns to 14:193/222 of 1l8lA
- active site: D17 (= D78), V18 (≠ M79), D19 (= D80), G107 (= G168), K155 (= K212), D180 (= D239)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D78), D19 (= D80), G107 (= G168), K155 (= K212), D176 (= D235), G177 (= G236), T179 (≠ N238)
6hyjB Psph human phosphoserine phosphatase (see paper)
28% identity, 64% coverage: 75:252/280 of query aligns to 17:196/223 of 6hyjB
Sites not aligning to the query:
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
28% identity, 64% coverage: 75:252/280 of query aligns to 17:196/225 of P78330
- D20 (= D78) binding
- DVD 20:22 (≠ DMD 78:80) binding
- D22 (= D80) binding
- S23 (= S81) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E87) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D90) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A93) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M110) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R111) binding
- R65 (= R123) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 167:169) binding ; binding
- N133 (≠ T187) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K212) binding ; binding
- D179 (= D235) binding
- T182 (≠ N238) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
Sites not aligning to the query:
- 202 R→A: Reduces L-phosphoserine phosphatase activity by about 99%.; R→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)
29% identity, 63% coverage: 76:251/280 of query aligns to 13:174/200 of 4ap9A
- active site: D15 (= D78), I16 (≠ M79), E17 (≠ D80), G103 (= G168), K141 (= K212), D162 (= D239)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ D94), I32 (≠ F95), T33 (≠ A96), L46 (≠ M110), W52 (≠ Y116), D140 (≠ A211), K141 (= K212), Y160 (≠ A237), A161 (≠ N238)
3kd3A Crystal structure of a phosphoserine phosphohydrolase-like protein from francisella tularensis subsp. Tularensis schu s4
31% identity, 64% coverage: 75:254/280 of query aligns to 4:187/216 of 3kd3A
Query Sequence
>Dsui_2379 FitnessBrowser__PS:Dsui_2379
MNLIIQNGALPTFLLDRIAAATQAAAVEPRPPRVVCFRNASRTTEFDALLPLIEAEKLDW
AFVPADRKLADYGLICFDMDSTLITIECIDELADFAGKKAEVSAVTESAMRGEIDYRESL
RRRLALLAGLDARVLARVYGERLLLSEGARELLEAAQTAGLRTAILSGGFTYFTERLRIE
LGFDFATSNELEISGGKLTGKVVGDIVDAQAKAHHLNRLRDELGLEREQVIAVGDGANDL
LMMAEAGLSVAFHAKPATRAKASVAISHGGLDSLLNLFEA
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