SitesBLAST
Comparing Echvi_3767 FitnessBrowser__Cola:Echvi_3767 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
3dr2A Structural and functional analyses of xc5397 from xanthomonas campestris: a gluconolactonase important in glucose secondary metabolic pathways (see paper)
30% identity, 88% coverage: 31:333/344 of query aligns to 10:288/299 of 3dr2A
3e5zA X-ray structure of the putative gluconolactonase in protein family pf08450. Northeast structural genomics consortium target drr130.
28% identity, 85% coverage: 50:342/344 of query aligns to 10:282/290 of 3e5zA
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
24% identity, 78% coverage: 69:337/344 of query aligns to 20:289/314 of 3o4pA
- active site: E21 (= E70), E37 (vs. gap), N120 (= N172), N175 (= N224), D229 (= D281), H287 (= H335)
- binding calcium ion: E21 (= E70), N120 (= N172), N175 (= N224), D229 (= D281), D232 (≠ K284), L273 (≠ C321), H274 (≠ T322)
- binding 1,2-dimethoxyethane: W244 (vs. gap), K269 (≠ L317), H287 (= H335)
- binding 2-methoxyethanol: K151 (vs. gap), T169 (≠ S219), A170 (vs. gap), F171 (≠ L220), E194 (≠ N239), W201 (≠ F248), E212 (≠ D259), N213 (≠ T260), K214 (≠ R261), K214 (≠ R261)
Sites not aligning to the query:
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.1.8.2 from Loligo vulgaris (Common European squid) (see 4 papers)
24% identity, 78% coverage: 69:337/344 of query aligns to 20:289/314 of Q7SIG4
- E21 (= E70) mutation to Q: 100% decrease in activity. Loss of calcium 1 binding.
- E37 (vs. gap) mutation to Q: 50% decrease in activity.
- Q77 (≠ L125) mutation to F: 100% decrease in activity.; mutation to W: No effect on activity.; mutation to Y: 6% increase in activity.
- N120 (= N172) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (= D173) mutation to F: 100% decrease in activity.
- Y144 (≠ A196) mutation to S: 8% increase in activity.
- R146 (≠ K198) mutation to S: 45% decrease in activity.
- M148 (≠ L200) mutation to A: 26% decrease in activity.
- F173 (≠ R222) mutation to A: 84% decrease in activity.; mutation to L: 28% decrease in activity.; mutation to S: 68% decrease in activity.; mutation to V: 46% decrease in activity.; mutation to W: 19% decrease in activity.; mutation to Y: 53% decrease in activity.
- N175 (= N224) mutation to D: 98% decrease in activity.
- H181 (≠ P230) mutation to N: 20% decrease in activity.
- T195 (≠ S240) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (≠ D266) mutation to N: 3% increase in activity.
- H224 (≠ R276) mutation to N: 14% increase in activity.
- D229 (= D281) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (≠ K284) binding ; mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G289) mutation to S: 4% decrease in activity.
- W244 (vs. gap) mutation to F: 44% decrease in activity.; mutation to H: 27% decrease in activity.; mutation to L: 62% decrease in activity.; mutation to Y: No effect on activity.
- H248 (vs. gap) mutation to N: 4% increase in activity.
- S271 (= S319) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (= N320) mutation to F: 100% decrease in activity.
- L273 (≠ C321) binding
- H274 (≠ T322) binding ; mutation to N: 85% decrease in activity.
- H287 (= H335) active site, Proton acceptor; mutation to A: 90% decrease in activity.; mutation to F: 36% decrease in activity.; mutation to L: 21% decrease in activity.; mutation to N: 97% decrease in activity.; mutation to Q: 54% decrease in activity.; mutation to W: 44% decrease in activity.; mutation to Y: 57% decrease in activity.
Sites not aligning to the query:
- 304 Q→F: 50% decrease in activity.; Q→W: 3% decrease in activity.
- 314 F→A: 3% increase in activity.
2gvvA Structure of diisopropyl fluorophosphatase (dfpase) in complex with dicyclopentylphosphoroamidate (dcppa) (see paper)
24% identity, 78% coverage: 69:337/344 of query aligns to 18:287/309 of 2gvvA
- active site: E19 (= E70), E35 (vs. gap), N118 (= N172), N173 (= N224), D227 (= D281), H285 (= H335)
- binding calcium ion: E19 (= E70), N118 (= N172), N173 (= N224), D227 (= D281), D230 (≠ K284), L271 (≠ C321), H272 (≠ T322)
- binding dicyclopentyl phosphoramidate: E19 (= E70), P34 (vs. gap), N118 (= N172), N173 (= N224), D227 (= D281), W242 (vs. gap), H285 (= H335)
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
25% identity, 78% coverage: 70:336/344 of query aligns to 17:254/289 of Q9A9Z1
- E17 (= E70) binding
- N145 (= N224) binding
- D195 (= D281) binding
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
25% identity, 78% coverage: 70:336/344 of query aligns to 17:254/289 of 7plbB
- binding fe (ii) ion: E17 (= E70), N100 (= N172), N145 (= N224), D195 (= D281)
- binding beta-D-xylopyranose: E17 (= E70), E89 (≠ H161), V90 (≠ D162), E91 (≠ Y163), D92 (≠ Q164), R98 (≠ S170), N100 (= N172), R109 (≠ N181), M115 (≠ R194), E119 (≠ K198), R128 (≠ C207), D130 (≠ K209), T132 (≠ N211), N145 (= N224), D174 (≠ P255), D195 (= D281), W210 (vs. gap)
- binding alpha-D-xylopyranose: H22 (≠ K77), A64 (≠ G138), T65 (≠ N139), G66 (≠ R140), F67 (≠ K141), H79 (vs. gap), P80 (= P152)
Sites not aligning to the query:
7pldA Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
25% identity, 78% coverage: 70:336/344 of query aligns to 15:252/287 of 7pldA
Sites not aligning to the query:
7rizA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound 2-hydroxyquinoline (see paper)
25% identity, 80% coverage: 59:333/344 of query aligns to 1:282/306 of 7rizA
- binding calcium ion: E12 (= E70), N120 (= N172), N169 (= N224), D226 (= D281), S227 (≠ G282)
- binding quinolin-2(1h)-one: F10 (≠ W68), E12 (= E70), N52 (= N122), F70 (≠ R140), P81 (vs. gap), N120 (= N172), L135 (= L191), N169 (= N224), D226 (= D281), L241 (≠ G295)
7risA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound phosphate (see paper)
30% identity, 48% coverage: 168:333/344 of query aligns to 107:269/293 of 7risA
Sites not aligning to the query:
8dk0A Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound (s)gamma- valerolactone (see paper)
29% identity, 48% coverage: 168:333/344 of query aligns to 111:269/293 of 8dk0A
Sites not aligning to the query:
8djzA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound product (see paper)
29% identity, 48% coverage: 168:333/344 of query aligns to 111:269/293 of 8djzA
Sites not aligning to the query:
8djfA Crystal structure of rpa3624, a beta-propeller lactonase from rhodopseudomonas palustris, with active-site bound tetrahedral intermediate (see paper)
29% identity, 48% coverage: 168:333/344 of query aligns to 111:269/293 of 8djfA
Sites not aligning to the query:
Query Sequence
>Echvi_3767 FitnessBrowser__Cola:Echvi_3767
MNLKPMLIGWLLVTAFGCSDQQKTSQVSKHAIPTSSEKPFSIEILDDQALKVISRDATIE
RMASGFDWVEGPLWIGKGDYLLFSDIPRNKVYKMTSEGDTSTYLNRSGYSGEGAYSREPG
SNALLLDKDNQLVLMQHGNRKVAKMKGGLDAPAPDFTSLVHDYQGKRLNSPNDGIFDKQG
NLYFTDPPYGLPPRFAGKELSFQGIYCLKTNGTLVLLDSLSRPNGIALSPDEKHLFVANS
DEKNAAWFQYPLEAPGEVDTRSLFYDATEEVLPGGRNGLPDGMKVHPKGYLFATGPDGIW
IFDLKGKVLGKIHTGQLTSNCTFTDDYKHLYVTAHRDILRVDLK
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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