SitesBLAST
Comparing 15057 FitnessBrowser__Keio:15057 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 81% coverage: 10:216/255 of query aligns to 15:231/378 of P69874
- C26 (≠ H20) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y21) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F39) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ G48) mutation to T: Loss of ATPase activity and transport.
- L60 (= L54) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ A70) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V120) mutation to M: Loss of ATPase activity and transport.
- D172 (= D157) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
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, 78% coverage: 14:212/255 of query aligns to 6:213/369 of P19566
- L86 (= L91) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P159) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D164) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 78% coverage: 14:212/255 of query aligns to 5:212/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 78% coverage: 14:212/255 of query aligns to 3:210/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y21), S35 (= S46), G36 (= G47), C37 (≠ G48), G38 (= G49), K39 (= K50), S40 (= S51), T41 (= T52), R126 (≠ E128), A130 (= A132), S132 (= S134), G134 (= G136), Q135 (= Q137)
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, 78% coverage: 14:212/255 of query aligns to 5:212/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y21), S37 (= S46), G38 (= G47), C39 (≠ G48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), Q81 (= Q87), R128 (≠ E128), A132 (= A132), S134 (= S134), G136 (= G136), Q137 (= Q137), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 78% coverage: 14:212/255 of query aligns to 5:212/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), G38 (= G47), C39 (≠ G48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ E128), S134 (= S134), Q137 (= Q137)
- binding beryllium trifluoride ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q87), S134 (= S134), G136 (= G136), H191 (= H191)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 78% coverage: 14:212/255 of query aligns to 5:212/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (= V26), G38 (= G47), C39 (≠ G48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ E128), A132 (= A132), S134 (= S134), Q137 (= Q137)
- binding tetrafluoroaluminate ion: S37 (= S46), G38 (= G47), K41 (= K50), Q81 (= Q87), S134 (= S134), G135 (= G135), G136 (= G136), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 78% coverage: 14:212/255 of query aligns to 5:212/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y21), V17 (= V26), G38 (= G47), C39 (≠ G48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ E128), A132 (= A132), S134 (= S134), Q137 (= Q137)
- binding magnesium ion: S42 (= S51), Q81 (= Q87)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 78% coverage: 14:212/255 of query aligns to 6:213/371 of P68187
- A85 (≠ R90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ W109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E123) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G136) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D157) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
35% identity, 77% coverage: 15:211/255 of query aligns to 30:241/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
35% identity, 77% coverage: 15:211/255 of query aligns to 30:241/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
34% identity, 77% coverage: 15:211/255 of query aligns to 30:241/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ N24), S61 (= S46), G62 (= G47), G64 (= G49), K65 (= K50), S66 (= S51), T67 (= T52), Q111 (= Q87), K161 (≠ A131), Q162 (≠ A132), S164 (= S134), G166 (= G136), M167 (≠ Q137), Q188 (≠ E158), H221 (= H191)
Sites not aligning to the query:
A5U7B7 Cell division ATP-binding protein FtsE from Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) (see 2 papers)
38% identity, 80% coverage: 12:214/255 of query aligns to 2:219/229 of A5U7B7
- K42 (= K50) mutation to R: Does not bind ATP. Does not affect dimerization.
- C84 (≠ M84) mutation to A: Does not affect ATPase activity.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 76% coverage: 19:211/255 of query aligns to 14:221/375 of 2d62A
8igqA Cryo-em structure of mycobacterium tuberculosis adp bound ftsex/ripc complex in peptidisc (see paper)
38% identity, 80% coverage: 12:214/255 of query aligns to 3:220/227 of 8igqA
8iddA Cryo-em structure of mycobacterium tuberculosis atp bound ftsex/ripc complex in peptidisc (see paper)
38% identity, 80% coverage: 12:214/255 of query aligns to 3:220/225 of 8iddA
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
38% identity, 78% coverage: 14:211/255 of query aligns to 9:207/353 of 1vciA
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 73% coverage: 27:211/255 of query aligns to 21:219/343 of P30750
- 40:46 (vs. 46:52, 86% identical) binding
- E166 (= E158) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
36% identity, 78% coverage: 12:211/255 of query aligns to 2:214/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y21), V16 (= V26), S36 (= S46), G37 (= G47), S38 (≠ G48), G39 (= G49), K40 (= K50), S41 (= S51), T42 (= T52), E162 (= E158), H194 (= H191)
- binding magnesium ion: S41 (= S51), E162 (= E158)
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 74% coverage: 23:211/255 of query aligns to 12:206/348 of 3d31A
Sites not aligning to the query:
Query Sequence
>15057 FitnessBrowser__Keio:15057
MNTARLNQGTPLLLNAVSKHYAENIVLNQLDLHIPAGQFVAVVGRSGGGKSTLLRLLAGL
ETPTAGDVLAGTTPLAEIQEDTRMMFQDARLLPWKSVIDNVGLGLKGQWRDAARRALAAV
GLENRAGEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRLEMQDLIVSLWQ
EHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDIPRPRRLGSVRLAELEAEVLQR
VMQRGESETRLRKQG
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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