SitesBLAST
Comparing N515DRAFT_0576 FitnessBrowser__Dyella79:N515DRAFT_0576 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
Q8L7R2 Homoserine kinase; Protein DOWNY MILDEW RESISTANT 1; EC 2.7.1.39 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 92% coverage: 5:306/330 of query aligns to 42:346/370 of Q8L7R2
- E46 (≠ N9) mutation to K: In dmr1-2; loss of function.
- G118 (= G84) mutation to R: In dmr1-6; loss of function.
- G180 (≠ A145) mutation to D: In dmr1-5; loss of function.
- G202 (= G168) mutation to R: In dmr1-4; loss of function.
- M241 (≠ A202) mutation to K: In dmr1-3; loss of function.
- A267 (≠ G228) mutation to V: In dmr1-1; loss of function.
P00547 Homoserine kinase; HK; HSK; EC 2.7.1.39 from Escherichia coli (strain K12) (see paper)
31% identity, 85% coverage: 24:304/330 of query aligns to 3:289/310 of P00547
- H139 (= H157) mutation to L: 35-fold decrease in kinase activity.
- H203 (≠ Q218) mutation to L: 2-fold decrease in kinase activity but nearly no change in substrates affinity.
- H206 (≠ N221) mutation to Q: 3500-fold decrease in kinase activity.
- R235 (= R250) mutation to H: 250-fold decrease in kinase activity but no change in substrates affinity.; mutation to L: 26200-fold decrease in catalytic efficiency.
1h74B Crystal structure of homoserine kinase complexed with ile (see paper)
28% identity, 80% coverage: 21:284/330 of query aligns to 1:264/296 of 1h74B
- active site: E126 (= E149), T179 (= T199)
- binding phosphothiophosphoric acid-adenylate ester: N58 (= N81), V59 (≠ T82), K83 (= K106), A87 (≠ L110), G88 (= G111), G90 (= G113), G92 (= G115), S93 (≠ G116), S94 (= S117), S97 (= S120), S129 (≠ A152)
- binding isoleucine: A12 (≠ G32), N13 (= N33), D19 (= D39), H134 (= H157), D136 (= D159), N137 (= N160), R183 (= R203), R231 (= R250), G256 (= G276)
1h74A Crystal structure of homoserine kinase complexed with ile (see paper)
28% identity, 80% coverage: 21:284/330 of query aligns to 1:264/296 of 1h74A
- active site: E126 (= E149), T179 (= T199)
- binding adenosine-5'-diphosphate: I51 (≠ L74), N58 (= N81), V59 (≠ T82), K83 (= K106), A87 (≠ L110), G88 (= G111), S93 (≠ G116), S94 (= S117), S97 (= S120), T179 (= T199)
- binding isoleucine: N13 (= N33), F18 (= F38), D19 (= D39), H134 (= H157), T179 (= T199), R183 (= R203), R231 (= R250)
1h73A Crystal structure of homoserine kinase complexed with threonine (see paper)
28% identity, 80% coverage: 21:284/330 of query aligns to 1:264/296 of 1h73A
- active site: E126 (= E149), T179 (= T199)
- binding phosphoaminophosphonic acid-adenylate ester: I51 (≠ L74), N58 (= N81), V59 (≠ T82), K83 (= K106), A87 (≠ L110), G88 (= G111), G90 (= G113), L91 (≠ M114), G92 (= G115), S93 (≠ G116), S94 (= S117), S97 (= S120)
- binding threonine: N13 (= N33), D19 (= D39), R183 (= R203), R231 (= R250)
1h72C Crystal structure of homoserine kinase complexed with hse (see paper)
28% identity, 80% coverage: 21:284/330 of query aligns to 1:264/296 of 1h72C
- active site: E126 (= E149), T179 (= T199)
- binding phosphoaminophosphonic acid-adenylate ester: I51 (≠ L74), N58 (= N81), V59 (≠ T82), K83 (= K106), A87 (≠ L110), G88 (= G111), G90 (= G113), L91 (≠ M114), G92 (= G115), S93 (≠ G116), S94 (= S117), S97 (= S120), S129 (≠ A152), T179 (= T199), S257 (≠ A277)
- binding l-homoserine: N13 (= N33), F18 (= F38), D19 (= D39), D136 (= D159), N137 (= N160), R183 (= R203), R231 (= R250)
1fwkA Crystal structure of homoserine kinase complexed with adp (see paper)
28% identity, 80% coverage: 21:284/330 of query aligns to 1:264/296 of 1fwkA
Query Sequence
>N515DRAFT_0576 FitnessBrowser__Dyella79:N515DRAFT_0576
MNAQLAAQNPEPMARSPQRALSAQALAPASVGNVGIGFDILGHSVAGAGDRARVRRIDEP
VVRIAAIEGCVVDLPLDPAQNTAGMALMALRKALGLRHGFELVLHKGIALGSGMGGSASS
CVAALVAANALLERPLPMESLYGFALEGEAVASGGRHGDNVGPMLLGGLVLATRDRLVRV
PVPDAWHCALVHPHMVLETRKARAALAGAYQLGEFVAQSANLSLMLAGCWQGDAGLVREG
LNDVLVEPRRAPLIPGFARVKQAAMDHRAMGASISGAGPSVFGWFEQRDEAKAAAAAMAA
AFAEAGLDSDTLVSPIAGPSAALIDVERKA
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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