SitesBLAST
Comparing Dsui_0564 FitnessBrowser__PS:Dsui_0564 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 12:216/369 of P19566
- L86 (= L95) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D172) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 11:215/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y20), S37 (= S43), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), Q81 (= Q91), R128 (= R136), A132 (≠ K140), S134 (= S142), G136 (= G144), Q137 (≠ E145), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 11:215/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y20), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R136), S134 (= S142), Q137 (≠ E145)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q91), S134 (= S142), G136 (= G144), H191 (= H199)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 11:215/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y20), V17 (≠ L25), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R136), A132 (≠ K140), S134 (= S142), Q137 (≠ E145)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q91), S134 (= S142), G135 (= G143), G136 (= G144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 11:215/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y20), V17 (≠ L25), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R136), A132 (≠ K140), S134 (= S142), Q137 (≠ E145)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q91)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 11:215/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
43% identity, 56% coverage: 19:223/365 of query aligns to 12:216/371 of P68187
- A85 (≠ S94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ E116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L121) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A124) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E126) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G131) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G144) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 340 G→A: Maltose transport is affected but retains ability to interact with MalT.
- 346 G→S: Normal maltose transport but constitutive mal gene expression.
- 355 F→Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
43% identity, 56% coverage: 19:223/365 of query aligns to 9:213/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y20), S35 (= S43), G36 (= G44), C37 (≠ S45), G38 (= G46), K39 (= K47), S40 (≠ T48), T41 (= T49), R126 (= R136), A130 (≠ K140), S132 (= S142), G134 (= G144), Q135 (≠ E145)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
29% identity, 89% coverage: 20:343/365 of query aligns to 16:347/375 of 2d62A
3d31A Modbc from methanosarcina acetivorans (see paper)
33% identity, 89% coverage: 38:363/365 of query aligns to 30:344/348 of 3d31A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 54% coverage: 28:223/365 of query aligns to 37:230/378 of P69874
- F45 (≠ V36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L128) mutation to M: Loss of ATPase activity and transport.
- D172 (= D165) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 276 C→A: Lower ATPase activity and transport efficiency.
- 297 mutation E->K,D: Lower ATPase activity and transport efficiency.; E→Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
29% identity, 89% coverage: 19:343/365 of query aligns to 12:344/372 of 1g291
- binding magnesium ion: D69 (= D74), E71 (≠ D76), K72 (≠ H77), K79 (≠ H82), D80 (≠ R83), E292 (≠ R289), D293 (= D290)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (≠ S45), G41 (= G46), K42 (= K47), T43 (= T48), T44 (= T49)
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 51% coverage: 37:223/365 of query aligns to 24:185/344 of 2awnC
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
34% identity, 59% coverage: 9:223/365 of query aligns to 6:214/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
36% identity, 58% coverage: 20:231/365 of query aligns to 16:219/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
35% identity, 56% coverage: 19:223/365 of query aligns to 18:216/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (≠ T48), Q82 (= Q91), Q133 (≠ K140), G136 (= G143), G137 (= G144), Q138 (≠ E145), H192 (= H199)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q91)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
35% identity, 56% coverage: 19:223/365 of query aligns to 18:216/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S43), C40 (≠ S45), G41 (= G46), K42 (= K47), S43 (≠ T48), T44 (= T49), Q82 (= Q91), R129 (= R136), Q133 (≠ K140), S135 (= S142), G136 (= G143), G137 (= G144), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q91)
Sites not aligning to the query:
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 52% coverage: 28:217/365 of query aligns to 24:211/393 of P9WQI3
- H193 (= H199) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 73% coverage: 38:304/365 of query aligns to 35:295/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 73% coverage: 38:304/365 of query aligns to 35:295/353 of 1oxvA
Sites not aligning to the query:
Query Sequence
>Dsui_0564 FitnessBrowser__PS:Dsui_0564
MATEMPNDDQAIRARFHIAYGEFSLAADLTLPGRGVTALFGHSGSGKTTLLRAIAGLERH
PGAYLEVNGEVWQDGDHFLPTHRRPLGYVFQEASLFPHLSVEANLDFGRKRLAAAERRVD
LAQAVELLGIGHLLARRPDKLSGGERQRVAIARALLASPRLLLMDEPLAALDGKRKAEIL
PYLTRLREELDIPVLYVTHSPDEVARLADHLVLLDNGQVAASGPLAETLARLDLPTAVSD
DAGVVVEGLVAGHDAAYHLLALDFPGGRVQVAHGPENPGKRLRFQVRARDVSLSLSERDD
SSILNRVPATVAAIADADTPAHVLVRLEAGGTPLLARITRRSRDQLQLQPGKNVWAQIKA
VALLA
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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