SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf1N1B4_3743 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3743 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 5 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)
24% identity, 95% coverage: 3:209/217 of query aligns to 181:371/409 of O53289

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O53289

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D185 (= D7) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
V186 (≠ L8) mutation to Q: Decreases enzymatic activity by 50%.
D187 (= D9) mutation to N: Decreases enzymatic activity by 15%.
S188 (≠ E10) mutation to A: No effect on enzymatic activity.
S273 (= S111) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
K318 (= K156) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
D341 (= D179) 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 (= D183) 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.

8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
23% identity, 95% coverage: 3:209/217 of query aligns to 179:369/396 of 8a21A

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binding magnesium ion: D183 (= D7), D185 (= D9), D339 (= D179)
binding 4-phenyl-1h-imidazole: D185 (= D9), E192 (≠ D16), V193 (≠ C17), I194 (≠ A18), T211 (≠ M44), M215 (≠ S48), F221 (≠ M54), R228 (≠ S61), G273 (≠ S113)

Sites not aligning to the query:

binding 4-phenyl-1h-imidazole: 13, 18, 37

8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
23% identity, 95% coverage: 3:209/217 of query aligns to 179:369/396 of 8a1zA

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binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D9), E192 (≠ D16), M215 (≠ S48), F221 (≠ M54), L225 (≠ M58), R228 (≠ S61), G272 (≠ A112), F274 (≠ G114), D339 (= D179)
binding magnesium ion: D183 (= D7), D185 (= D9), D339 (= D179)

5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
23% identity, 95% coverage: 3:209/217 of query aligns to 179:369/396 of 5jlpA

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active site: D183 (= D7), V184 (≠ L8), D185 (= D9), G272 (≠ A112), K316 (= K156), D343 (= D183)
binding magnesium ion: D183 (= D7), D339 (= D179)

Sites not aligning to the query:

binding serine: 13, 14

A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
23% identity, 95% coverage: 3:209/217 of query aligns to 183:373/411 of A0QJI1

query
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D187 (= D7) binding
D189 (= D9) binding
D343 (= D179) binding

Query Sequence

>Pf1N1B4_3743 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3743
MALAIFDLDETLIHGDCATLWSEQMGRLGWVDPESFMRQNNELMDAYSHGKLRMEEYMTF
SLEPMIGRTPEEVDHLVGPWVEDFIEPIIFSDATKAIAAHRKAGDRILVISASGTHLVKP
IADRLGIDEILGIELEVAHGVYSGNTVGTLTYREGKITRLLEWLDAEEENLEGASFYSDS
RNDLPLLLKVDFPHVVNPDPVLLEHAEKAGWPIHIWK

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