SitesBLAST
Comparing SM_b21572 FitnessBrowser__Smeli:SM_b21572 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 4 hits to proteins with known functional sites (download)
7yleA Rndmpx in complex with dmsp (see paper)
38% identity, 93% coverage: 25:333/333 of query aligns to 1:298/299 of 7yleA
4xz6A Tmox in complex with tmao (see paper)
24% identity, 88% coverage: 29:321/333 of query aligns to 6:289/291 of 4xz6A
- binding calcium ion: P207 (≠ D244), V209 (≠ P246), N212 (≠ K249), A215 (= A252), D218 (vs. gap)
- binding trimethylamine oxide: W13 (= W36), W60 (= W85), F64 (≠ L89), E89 (≠ Q115), W135 (= W161), F178 (≠ Y209), W180 (= W211)
Q5LT66 Trimethylamine N-oxide-binding protein; TMAO-binding protein from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
24% identity, 88% coverage: 29:321/333 of query aligns to 48:331/333 of Q5LT66
- W55 (= W36) binding ; mutation to A: Nearly complete abrogation of the TMAO-binding affinity.; mutation to F: Significant decrease in the TMAO-binding affinity.
- W102 (= W85) binding ; mutation to A: Nearly complete abrogation of the TMAO-binding affinity.; mutation to F: Significant decrease in the TMAO-binding affinity.
- F106 (≠ L89) mutation to A: Decrease in the TMAO-binding affinity.
- E131 (≠ Q115) binding ; mutation to A: Nearly complete abrogation of the TMAO-binding affinity.
- W177 (= W161) binding ; mutation to A: Nearly complete abrogation of the TMAO-binding affinity.; mutation to F: Significant decrease in the TMAO-binding affinity.
- F220 (≠ Y209) mutation to A: Significant decrease in the TMAO-binding affinity.
- W222 (= W211) binding ; mutation to A: Significant decrease in the TMAO-binding affinity.; mutation to F: Decrease in the TMAO-binding affinity.
- P249 (≠ D244) binding
- V251 (≠ P246) binding
- N254 (≠ K249) binding
- A257 (= A252) binding
- D260 (vs. gap) binding
Sites not aligning to the query:
Q4FL33 Trimethylamine N-oxide-binding protein; TMAO-binding protein from Pelagibacter ubique (strain HTCC1062) (see paper)
22% identity, 95% coverage: 1:318/333 of query aligns to 1:310/314 of Q4FL33
- W38 (= W36) mutation to A: Maintains a relatively high binding affinity toward TMAO.
- W85 (= W85) mutation to A: Severely decreases the binding affinity toward TMAO.
- F89 (≠ L89) mutation to A: Severely decreases the binding affinity toward TMAO.
- E114 (≠ P110) mutation to A: Abolishes the binding affinity toward TMAO.
- F210 (≠ Y209) mutation to A: Maintains a relatively high binding affinity toward TMAO.
- W212 (= W211) mutation to A: Severely decreases the binding affinity toward TMAO.
Query Sequence
>SM_b21572 FitnessBrowser__Smeli:SM_b21572
MKKLLASTCLMLGLIAGASTSSAAECGTVTIASMNWQSAEVLSNLDKFILNEGYGCSAEI
TIGDTVPTITSMAEKGQPDIAPEAWIDLLPDVVKKGQDDGRIITVGSPLPDGGVQGWWIP
QYLADAHPDIKTIGDALKHPELFPASEDPSKGAILNGPQGWGGTVVTTQLFSAFDGEKAG
FTLVDTGSAAGLDGAIAKAYERKEGLLTYYWSPTALLGKYKMVKLDPGVPHDAAEWKRCN
TVADCPDPKPNAWPVDTIVTLVAKPFSERVGPEVMDYLTKRSWSNETVSQLMAWMTDNQA
SGEEGAKRFLEENEDMWSKWVSPEAAEKIKAAL
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