SitesBLAST
Comparing H281DRAFT_05181 FitnessBrowser__Burk376:H281DRAFT_05181 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 20 (the maximum) hits to proteins with known functional sites (download)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 93% coverage: 30:388/388 of query aligns to 17:374/378 of P69874
- C26 (≠ K39) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F40) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L58) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C67) mutation to T: Loss of ATPase activity and transport.
- L60 (= L73) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I89) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V148) mutation to M: Loss of ATPase activity and transport.
- D172 (= D185) mutation to N: Loss of ATPase activity and transport.
- C276 (= C288) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E311) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
43% identity, 81% coverage: 31:346/388 of query aligns to 7:332/375 of 2d62A
1g291 Malk (see paper)
42% identity, 85% coverage: 31:359/388 of query aligns to 4:341/372 of 1g291
- binding magnesium ion: D69 (= D90), E71 (= E92), K72 (≠ D93), K79 (≠ Y100), D80 (≠ R101), E292 (= E311), D293 (≠ R312)
- binding pyrophosphate 2-: S38 (= S65), G39 (= G66), C40 (= C67), G41 (= G68), K42 (= K69), T43 (≠ S70), T44 (= T71)
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
41% identity, 82% coverage: 31:349/388 of query aligns to 3:321/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F40), S37 (= S65), G38 (= G66), C39 (= C67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), Q81 (= Q109), R128 (= R156), A132 (≠ Q160), S134 (= S162), G136 (= G164), Q137 (= Q165), E158 (= E186), H191 (= H219)
- binding magnesium ion: S42 (= S70), Q81 (= Q109)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 82% coverage: 31:349/388 of query aligns to 3:321/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F40), G38 (= G66), C39 (= C67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), R128 (= R156), S134 (= S162), Q137 (= Q165)
- binding beryllium trifluoride ion: S37 (= S65), G38 (= G66), K41 (= K69), Q81 (= Q109), S134 (= S162), G136 (= G164), H191 (= H219)
- binding magnesium ion: S42 (= S70), Q81 (= Q109)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 82% coverage: 31:349/388 of query aligns to 3:321/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F40), V17 (≠ A45), G38 (= G66), C39 (= C67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), R128 (= R156), A132 (≠ Q160), S134 (= S162), Q137 (= Q165)
- binding tetrafluoroaluminate ion: S37 (= S65), G38 (= G66), K41 (= K69), Q81 (= Q109), S134 (= S162), G135 (= G163), G136 (= G164), E158 (= E186), H191 (= H219)
- binding magnesium ion: S42 (= S70), Q81 (= Q109)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 82% coverage: 31:349/388 of query aligns to 3:321/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F40), V17 (≠ A45), G38 (= G66), C39 (= C67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), R128 (= R156), A132 (≠ Q160), S134 (= S162), Q137 (= Q165)
- binding magnesium ion: S42 (= S70), Q81 (= Q109)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 82% coverage: 31:349/388 of query aligns to 3:321/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 82% coverage: 31:349/388 of query aligns to 4:322/371 of P68187
- A85 (= A112) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P133) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V141) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A144) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E146) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G151) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G164) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D185) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R255) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L266) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ N293) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G301) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T305) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ S307) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G329) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A335) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (= S349) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
41% identity, 82% coverage: 31:349/388 of query aligns to 1:319/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F40), S35 (= S65), G36 (= G66), C37 (= C67), G38 (= G68), K39 (= K69), S40 (= S70), T41 (= T71), R126 (= R156), A130 (≠ Q160), S132 (= S162), G134 (= G164), Q135 (= Q165)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 82% coverage: 31:347/388 of query aligns to 4:318/369 of P19566
- L86 (= L113) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P187) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D192) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ A335) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
8hplC Lpqy-sugabc in state 1 (see paper)
46% identity, 61% coverage: 33:267/388 of query aligns to 4:240/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 82% coverage: 31:347/388 of query aligns to 7:311/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 57% coverage: 45:267/388 of query aligns to 18:242/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S65), G39 (= G66), G41 (= G68), K42 (= K69), S43 (= S70), Q82 (= Q109), Q133 (= Q160), G136 (= G163), G137 (= G164), Q138 (= Q165), H192 (= H219)
- binding magnesium ion: S43 (= S70), Q82 (= Q109)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 57% coverage: 45:267/388 of query aligns to 18:242/362 of 8hprD