SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 17206 FitnessBrowser__Keio:17206 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 2 hits to proteins with known functional sites (download)

P26380 PTS system fructose-specific EIIB component; EIIB-Fru; Fructose-specific phosphotransferase enzyme IIB component; lev-PTS; p18; EC 2.7.1.202 from Bacillus subtilis (strain 168) (see paper)
32% identity, 100% coverage: 1:157/157 of query aligns to 1:158/163 of P26380

query
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P26380

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H15 (= H15) active site, Pros-phosphohistidine intermediate; modified: Phosphohistidine; by EIIA; mutation to A: Unable to be phosphorylated.

P69797 PTS system mannose-specific EIIAB component; EIIAB-Man; EIII-Man; EC 2.7.1.191 from Escherichia coli (strain K12) (see 4 papers)
38% identity, 98% coverage: 4:157/157 of query aligns to 164:318/323 of P69797

query
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P69797

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H175 (= H15) mutation to C: Loss of phosphotransferase activity.
H219 (≠ R59) mutation to Q: Slight phosphotransferase activity.
K234 (≠ H71) modified: N6-acetyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
10 H→C: Loss of phosphotransferase activity. Unable to dimerize.; H→E: Results in the formation of a single complex corresponding to the productive phosphoryl transfer complex.
12 W→F: Slight phosphotransferase activity. Unable to dimerize.
48 K→C: Retains more than 50% of phosphotransferase activity.
55 modified: N6-acetyllysine
72 S→C: Slight phosphotransferase activity. Unable to dimerize.
86 H→N: Loss of phosphotransferase activity.
110 S→C: Retains more than 50% of phosphotransferase activity.

Query Sequence

>17206 FitnessBrowser__Keio:17206
MPNIVLSRIDERLIHGQVGVQWVGFAGANLVLVANDEVAEDPVQQNLMEMVLAEGIAVRF
WTLQKVIDNIHRAADRQKILLVCKTPADFLTLVKGGVPVNRINVGNMHYANGKQQIAKTV
SVDAGDIAAFNDLKTAGVECFVQGVPTEPAVDLFKLL

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