SitesBLAST

Comparing 203521 FitnessBrowser__MR1:203521 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

3d31A Modbc from methanosarcina acetivorans (see paper)
32% identity, 93% coverage: 24:366/367 of query aligns to 21:347/348 of 3d31A

• binding tungstate(vi)ion: S286 (≠ L300), I287 (≠ C301), R288 (= R302), I319 (≠ V338), T320 (≠ S339), S323 (≠ L342), K340 (= K359), A341 (≠ S360), S342 (≠ E361)

2d62A Crystal structure of multiple sugar binding transport atp- binding protein
31% identity, 93% coverage: 25:366/367 of query aligns to 28:366/375 of 2d62A

• binding pyrophosphate 2-: P40 (= P37), S41 (= S38), G42 (= G39), C43 (≠ G40), G44 (= G41), K45 (= K42), T46 (= T43), T47 (= T44)

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 62% coverage: 23:249/367 of query aligns to 37:259/378 of P69874

• F45 (≠ V31) mutation to L: Lower ATPase activity and transport efficiency.
• C54 (≠ G40) mutation to T: Loss of ATPase activity and transport.
• L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
• L76 (≠ F62) mutation to P: Lower ATPase activity and transport efficiency.
• V135 (= V125) mutation to M: Loss of ATPase activity and transport.
• D172 (= D162) 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.

1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
33% identity, 94% coverage: 24:367/367 of query aligns to 27:345/353 of 1vciA

• binding adenosine-5'-triphosphate: P40 (= P37), S41 (= S38), G42 (= G39), C43 (≠ G40), G44 (= G41), K45 (= K42), T46 (= T43), T47 (= T44)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 16, 19

7ahhC Opua inhibited inward-facing, sbd docked (see paper)
39% identity, 57% coverage: 24:234/367 of query aligns to 47:259/382 of 7ahhC

• binding phosphoaminophosphonic acid-adenylate ester: S61 (= S38), G62 (= G39), S63 (≠ G40), G64 (= G41), K65 (= K42), S66 (≠ T43), T67 (= T44), D187 (= D162), E188 (= E163)

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: 272, 273, 275, 295, 296, 297, 298, 357, 370, 372
• binding phosphoaminophosphonic acid-adenylate ester: 12, 29, 39, 40, 41

7aheC Opua inhibited inward facing (see paper)
39% identity, 57% coverage: 24:234/367 of query aligns to 47:259/382 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, 295, 296, 297, 298, 357, 372

1g291 Malk (see paper)
40% identity, 59% coverage: 25:239/367 of query aligns to 25:241/372 of 1g291

• binding magnesium ion: D69 (= D69), E71 (≠ K71), K72 (≠ S72), K79 (≠ Q79), D80 (≠ Q80), Y228 (≠ L226), D229 (≠ S227)
• binding pyrophosphate 2-: P37 (= P37), S38 (= S38), G39 (= G39), C40 (≠ G40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)

Sites not aligning to the query:

• binding magnesium ion: 292, 293, 341, 342, 359

7ahdC Opua (e190q) occluded (see paper)
39% identity, 57% coverage: 24:234/367 of query aligns to 47:259/260 of 7ahdC

• binding adenosine-5'-triphosphate: S61 (= S38), G62 (= G39), S63 (≠ G40), G64 (= G41), K65 (= K42), S66 (≠ T43), T67 (= T44), Q111 (= Q88), K161 (≠ M136), Q162 (≠ H137), S164 (= S139), G166 (= G141), M167 (≠ Q142), Q188 (≠ E163), H221 (= H196)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 12, 29, 39

2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
40% identity, 57% coverage: 29:239/367 of query aligns to 28:234/372 of 2awoA

• binding adenosine-5'-diphosphate: S37 (= S38), G38 (= G39), C39 (≠ G40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44)
• binding magnesium ion: S42 (≠ T43), D157 (= D162)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12, 17

3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
40% identity, 57% coverage: 29:239/367 of query aligns to 28:234/371 of 3puyA

• binding phosphoaminophosphonic acid-adenylate ester: P36 (= P37), S37 (= S38), G38 (= G39), C39 (≠ G40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), Q81 (= Q88), R128 (= R133), A132 (≠ H137), S134 (= S139), G135 (= G140), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
• binding magnesium ion: S42 (≠ T43), Q81 (= Q88), D157 (= D162)

Sites not aligning to the query:

• binding phosphoaminophosphonic acid-adenylate ester: 12, 17

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 57% coverage: 29:239/367 of query aligns to 28:234/371 of 3puxA

• binding adenosine-5'-diphosphate: S37 (= S38), G38 (= G39), C39 (≠ G40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R133), A132 (≠ H137), L133 (= L138), S134 (= S139), Q137 (= Q142)
• binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q88), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), H191 (= H196)
• binding magnesium ion: S42 (≠ T43), Q81 (= Q88), D157 (= D162)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12, 17

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 57% coverage: 29:239/367 of query aligns to 28:234/371 of 3puwA

• binding adenosine-5'-diphosphate: S37 (= S38), G38 (= G39), C39 (≠ G40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R133), A132 (≠ H137), S134 (= S139), Q137 (= Q142)
• binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q88), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), N162 (≠ A167), H191 (= H196)
• binding magnesium ion: S42 (≠ T43), Q81 (= Q88)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12, 17

2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 57% coverage: 29:239/367 of query aligns to 28:234/374 of 2awnB

• binding adenosine-5'-diphosphate: S37 (= S38), G38 (= G39), C39 (≠ G40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44)

Sites not aligning to the query:

• binding adenosine-5'-diphosphate: 12, 17

1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 57% coverage: 29:239/367 of query aligns to 26:232/367 of 1q12A

• binding adenosine-5'-triphosphate: S35 (= S38), G36 (= G39), C37 (≠ G40), G38 (= G41), K39 (= K42), S40 (≠ T43), T41 (= T44), R126 (= R133), K129 (≠ M136), A130 (≠ H137), L131 (= L138), S132 (= S139), G133 (= G140), G134 (= G141), Q135 (= Q142), N160 (≠ A167), H189 (= H196)

Sites not aligning to the query:

• binding adenosine-5'-triphosphate: 10, 15

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 57% coverage: 29:239/367 of query aligns to 29:235/371 of P68187

• A85 (≠ G91) mutation to M: Suppressor of EAA loop mutations in MalFG.
• K106 (≠ S112) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V114 (≠ A118) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V117 (≠ W121) mutation to M: Suppressor of EAA loop mutations in MalFG.
• E119 (≠ D123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• A124 (≠ Q128) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G137 (= G141) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
• D158 (= D162) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
• R228 (≠ E232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.

Sites not aligning to the query:

• 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.

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, 57% coverage: 29:239/367 of query aligns to 29:235/369 of P19566

• L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• P160 (= P164) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• D165 (= D169) 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.

1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 62% coverage: 21:248/367 of query aligns to 23:251/353 of 1oxvD

• binding phosphoaminophosphonic acid-adenylate ester: P39 (= P37), S40 (= S38), G41 (= G39), A42 (≠ G40), G43 (= G41), K44 (= K42), T45 (= T43), T46 (= T44), Q89 (= Q88), E166 (= E163)
• binding magnesium ion: T45 (= T43), Q89 (= Q88)

Sites not aligning to the query:

• binding phosphoaminophosphonic acid-adenylate ester: 13, 18, 20

1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 62% coverage: 21:248/367 of query aligns to 23:251/353 of 1oxvA

• binding phosphoaminophosphonic acid-adenylate ester: P39 (= P37), S40 (= S38), G41 (= G39), A42 (≠ G40), G43 (= G41), K44 (= K42), T45 (= T43), T46 (= T44), E166 (= E163)

Sites not aligning to the query:

• binding phosphoaminophosphonic acid-adenylate ester: 13, 18, 20

1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 62% coverage: 21:248/367 of query aligns to 23:251/353 of 1oxuA