SitesBLAST
Comparing HSERO_RS15175 FitnessBrowser__HerbieS:HSERO_RS15175 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)
40% identity, 80% coverage: 60:293/294 of query aligns to 140:384/409 of O53289
- D185 (= D93) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M94) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D95) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S96) mutation to A: No effect on enzymatic activity.
- S273 (= S182) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K227) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D250) 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 (= D254) 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.
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
40% identity, 81% coverage: 54:292/294 of query aligns to 44:285/295 of 7qplA
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
40% identity, 81% coverage: 57:293/294 of query aligns to 147:382/396 of 8a21A
- binding magnesium ion: D183 (= D93), D185 (= D95), D339 (= D250)
- binding 4-phenyl-1h-imidazole: D185 (= D95), E192 (= E102), V193 (≠ C103), I194 (= I104), T211 (= T121), M215 (= M125), F221 (= F131), R228 (= R138), G273 (= G184)
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)
40% identity, 81% coverage: 57:293/294 of query aligns to 147:382/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D95), E192 (= E102), M215 (= M125), F221 (= F131), L225 (= L135), R228 (= R138), G272 (= G183), F274 (= F185), D339 (= D250)
- binding magnesium ion: D183 (= D93), D185 (= D95), D339 (= D250)
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
40% identity, 80% coverage: 59:293/294 of query aligns to 153:386/411 of A0QJI1
- D187 (= D93) binding
- D189 (= D95) binding
- D343 (= D250) binding
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
40% identity, 80% coverage: 59:293/294 of query aligns to 149:382/396 of 5jlpA
Sites not aligning to the query:
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
37% identity, 70% coverage: 88:293/294 of query aligns to 5:209/210 of 1f5sA
- active site: D10 (= D93), F11 (≠ M94), D12 (= D95), G99 (= G183), K143 (= K227), D170 (= D254)
- binding magnesium ion: D10 (= D93), D12 (= D95), D166 (= D250)
- binding phosphate ion: D10 (= D93), F11 (≠ M94), D12 (= D95), S98 (= S182), G99 (= G183), K143 (= K227)
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)
37% identity, 70% coverage: 88:293/294 of query aligns to 6:210/211 of Q58989
- D11 (= D93) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D95) active site, Proton donor; binding
- E20 (= E102) binding
- R56 (= R138) binding
- SG 99:100 (= SG 182:183) binding
- K144 (= K227) binding
- D167 (= D250) binding
- N170 (= N253) binding
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
37% identity, 70% coverage: 88:293/294 of query aligns to 4:208/209 of 1l7nA
- active site: D9 (= D93), F10 (≠ M94), D11 (= D95), G98 (= G183), K142 (= K227), D169 (= D254)
- binding aluminum fluoride: D9 (= D93), F10 (≠ M94), D11 (= D95), S97 (= S182), K142 (= K227)
- binding tetrafluoroaluminate ion: D9 (= D93), F10 (≠ M94), D11 (= D95), S97 (= S182), G98 (= G183), K142 (= K227), N168 (= N253)
- binding magnesium ion: D9 (= D93), D11 (= D95), D165 (= D250)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
37% identity, 70% coverage: 88:293/294 of query aligns to 3:207/208 of 1l7pA
- active site: N8 (≠ D93), F9 (≠ M94), D10 (= D95), G97 (= G183), K141 (= K227), D168 (= D254)
- binding phosphoserine: N8 (≠ D93), F9 (≠ M94), D10 (= D95), E17 (= E102), M40 (= M125), F46 (= F131), R53 (= R138), S96 (= S182), G97 (= G183), K141 (= K227)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
35% identity, 70% coverage: 88:293/294 of query aligns to 3:199/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
34% identity, 66% coverage: 88:282/294 of query aligns to 4:196/208 of 3m1yC
6hyjB Psph human phosphoserine phosphatase (see paper)
29% identity, 56% coverage: 90:255/294 of query aligns to 17:184/223 of 6hyjB
Sites not aligning to the query:
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
28% identity, 64% coverage: 90:276/294 of query aligns to 13:200/217 of 6q6jB
- binding calcium ion: D16 (= D93), D18 (= D95), D175 (= D250)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D93), V17 (≠ M94), D18 (= D95), F54 (= F131), S105 (= S182), G106 (= G183), G107 (= G184), K154 (vs. gap), T178 (≠ N253)
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
28% identity, 64% coverage: 90:276/294 of query aligns to 14:201/222 of 1l8oA
- active site: D17 (= D93), V18 (≠ M94), D19 (= D95), G107 (= G183), K155 (vs. gap), D180 (= D254)
- binding phosphate ion: D17 (= D93), D19 (= D95), S106 (= S182), K155 (vs. gap)
- binding serine: G177 (= G251), T179 (≠ N253), R199 (= R274)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
28% identity, 64% coverage: 90:276/294 of query aligns to 14:201/222 of 1l8lA
- active site: D17 (= D93), V18 (≠ M94), D19 (= D95), G107 (= G183), K155 (vs. gap), D180 (= D254)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D93), D19 (= D95), G107 (= G183), K155 (vs. gap), D176 (= D250), G177 (= G251), T179 (≠ N253)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
29% identity, 56% coverage: 90:255/294 of query aligns to 17:184/225 of P78330
- D20 (= D93) binding
- DVD 20:22 (≠ DMD 93:95) binding
- D22 (= D95) binding
- S23 (= S96) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E102) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D105) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A108) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M125) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R126) binding
- R65 (= R138) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 182:184) binding ; binding
- N133 (≠ G211) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (vs. gap) binding ; binding
- D179 (= D250) binding
- T182 (≠ N253) 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%.
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
28% identity, 64% coverage: 90:276/294 of query aligns to 13:200/221 of 6hyyA
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
32% identity, 44% coverage: 88:215/294 of query aligns to 10:133/200 of 4ap9A
Sites not aligning to the query:
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
27% identity, 57% coverage: 90:258/294 of query aligns to 17:183/585 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
>HSERO_RS15175 FitnessBrowser__HerbieS:HSERO_RS15175
MNQQNNMNLILQAPKQHAVSSSAIEAIAALAGGDVERISDARVPDADVWRVAGVSLNEAL
KASVDAACLQARLDYAFIDADRKLADFRLVAMDMDSTLITIECIDEIADMQGLKPQVAEI
TEAAMRGEIEFNESLTRRVALLKGLDAGALQRVYDERLQLSPGAENMLKAVQAAGLKTLL
VSGGFTFFTDRMKARLNLDYTHANTLEVVDGKLTGKVVGGIVNADEKRATVERVCREIGA
EPTQAIVMGDGANDLRMMGISGLSVAFRAKPVVRAQASVGLNFVGLDGILNLLA
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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