SitesBLAST
Comparing WP_020565838.1 NCBI__GCF_000372865.1:WP_020565838.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
6hyjB Psph human phosphoserine phosphatase (see paper)
39% identity, 93% coverage: 2:199/213 of query aligns to 13:212/223 of 6hyjB
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
39% identity, 93% coverage: 2:199/213 of query aligns to 9:208/217 of 6q6jB
- binding calcium ion: D16 (= D9), D18 (= D11), D175 (= D166)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D9), V17 (≠ C10), D18 (= D11), F54 (≠ L47), S105 (= S98), G106 (= G99), G107 (= G100), K154 (= K147), T178 (= T169)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
39% identity, 93% coverage: 2:199/213 of query aligns to 13:212/225 of P78330
- D20 (= D9) binding Mg(2+)
- DVD 20:22 (≠ DCD 9:11) binding L-serine
- D22 (= D11) binding Mg(2+)
- S23 (= S12) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E18) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D21) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A24) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M41) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ N42) binding phosphate
- R65 (= R54) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 98:100) binding L-serine; binding O-phospho-L-serine
- N133 (≠ V122) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K147) binding L-serine; binding O-phospho-L-serine
- D179 (= D166) binding Mg(2+)
- T182 (= T169) binding O-phospho-L-serine; binding phosphate; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
- R202 (= R189) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
39% identity, 93% coverage: 2:199/213 of query aligns to 9:208/221 of 6hyyA
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
39% identity, 93% coverage: 2:199/213 of query aligns to 10:209/222 of 1l8oA
- active site: D17 (= D9), V18 (≠ C10), D19 (= D11), G107 (= G99), K155 (= K147), D180 (= D170)
- binding phosphate ion: D17 (= D9), D19 (= D11), S106 (= S98), K155 (= K147)
- binding serine: G177 (= G167), T179 (= T169), R199 (= R189)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
39% identity, 93% coverage: 2:199/213 of query aligns to 10:209/222 of 1l8lA
- active site: D17 (= D9), V18 (≠ C10), D19 (= D11), G107 (= G99), K155 (= K147), D180 (= D170)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D9), D19 (= D11), G107 (= G99), K155 (= K147), D176 (= D166), G177 (= G167), T179 (= T169)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
31% identity, 92% coverage: 4:199/213 of query aligns to 15:212/585 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
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
31% identity, 98% coverage: 5:212/213 of query aligns to 5:208/209 of 1l7nA
- active site: D9 (= D9), F10 (≠ C10), D11 (= D11), G98 (= G99), K142 (= K147), D169 (= D170)
- binding aluminum fluoride: D9 (= D9), F10 (≠ C10), D11 (= D11), S97 (= S98), K142 (= K147)
- binding tetrafluoroaluminate ion: D9 (= D9), F10 (≠ C10), D11 (= D11), S97 (= S98), G98 (= G99), K142 (= K147), N168 (≠ T169)
- binding magnesium ion: D9 (= D9), D11 (= D11), D165 (= D166)
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)
31% identity, 98% coverage: 5:212/213 of query aligns to 7:210/211 of Q58989
- D11 (= D9) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
- D13 (= D11) active site, Proton donor; binding Mg(2+)
- E20 (= E18) binding substrate
- R56 (= R54) binding substrate
- SG 99:100 (= SG 98:99) binding substrate
- K144 (= K147) binding substrate
- D167 (= D166) binding Mg(2+)
- N170 (≠ T169) binding substrate
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
31% identity, 98% coverage: 5:212/213 of query aligns to 6:209/210 of 1f5sA
- active site: D10 (= D9), F11 (≠ C10), D12 (= D11), G99 (= G99), K143 (= K147), D170 (= D170)
- binding magnesium ion: D10 (= D9), D12 (= D11), D166 (= D166)
- binding phosphate ion: D10 (= D9), F11 (≠ C10), D12 (= D11), S98 (= S98), G99 (= G99), K143 (= K147)
3kd3A Crystal structure of a phosphoserine phosphohydrolase-like protein from francisella tularensis subsp. Tularensis schu s4
28% identity, 91% coverage: 6:198/213 of query aligns to 4:203/216 of 3kd3A
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
30% identity, 98% coverage: 5:212/213 of query aligns to 4:207/208 of 1l7pA
- active site: N8 (≠ D9), F9 (≠ C10), D10 (= D11), G97 (= G99), K141 (= K147), D168 (= D170)
- binding phosphoserine: N8 (≠ D9), F9 (≠ C10), D10 (= D11), E17 (= E18), M40 (= M41), F46 (≠ L47), R53 (= R54), S96 (= S98), G97 (= G99), K141 (= K147)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
29% identity, 98% coverage: 5:212/213 of query aligns to 4:199/200 of 1l7oA
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
30% identity, 96% coverage: 5:209/213 of query aligns to 179:379/396 of 5jlpA
Sites not aligning to the query:
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
30% identity, 96% coverage: 5:209/213 of query aligns to 183:383/411 of A0QJI1
- D187 (= D9) binding Mg(2+)
- D189 (= D11) binding Mg(2+)
- D343 (= D166) binding Mg(2+)
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
30% identity, 96% coverage: 5:209/213 of query aligns to 179:379/396 of 8a21A
- binding magnesium ion: D183 (= D9), D185 (= D11), D339 (= D166)
- binding 4-phenyl-1h-imidazole: D185 (= D11), E192 (= E18), V193 (≠ G19), I194 (= I20), T211 (= T37), M215 (= M41), F221 (≠ L47), R228 (= R54), G273 (= G100)
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)
30% identity, 96% coverage: 5:209/213 of query aligns to 179:379/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D11), E192 (= E18), M215 (= M41), F221 (≠ L47), L225 (≠ Y51), R228 (= R54), G272 (= G99), F274 (≠ I101), D339 (= D166)
- binding magnesium ion: D183 (= D9), D185 (= D11), D339 (= D166)
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)
30% identity, 96% coverage: 5:209/213 of query aligns to 181:381/409 of O53289
- D185 (= D9) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ C10) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D11) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S12) mutation to A: No effect on enzymatic activity.
- S273 (= S98) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K147) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D166) 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 (= D170) 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
26% identity, 96% coverage: 5:209/213 of query aligns to 82:283/295 of 7qplA
Query Sequence
>WP_020565838.1 NCBI__GCF_000372865.1:WP_020565838.1
MSFDVICFDCDSTLSKIEGIDELAGRVGLGEEMSRLTDAAMNGLVPLEAVYEKRLSLIRP
DRAGIDWLARLYISEIVEGAAEVFSSLSARNKELHIISGGIRQAILPLAGFLGLPESRVH
AVDVYFNEDGSYRGYDQSSPLARTGGKAEICRRLVKPEVPLLMIGDGKTDMEAKQEGVSV
IGFGGVVARPIVRELADFYFDHPTLLPILSYIL
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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