SitesBLAST

Comparing GFF3902 FitnessBrowser__Marino:GFF3902 to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

2d62A Crystal structure of multiple sugar binding transport atp- binding protein
36% identity, 92% coverage: 28:369/371 of query aligns to 12:366/375 of 2d62A

• binding pyrophosphate 2-: P40 (= P56), S41 (= S57), G42 (= G58), C43 (= C59), G44 (= G60), K45 (= K61), T46 (= T62), T47 (= T63)

1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 75% coverage: 23:302/371 of query aligns to 4:285/353 of 1oxvD

• binding phosphoaminophosphonic acid-adenylate ester: F13 (= F32), V18 (= V37), A20 (vs. gap), P39 (= P56), S40 (= S57), G41 (= G58), A42 (≠ C59), G43 (= G60), K44 (= K61), T45 (= T62), T46 (= T63), Q89 (= Q106), E166 (= E181)
• binding magnesium ion: T45 (= T62), Q89 (= Q106)

1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 75% coverage: 23:302/371 of query aligns to 4:285/353 of 1oxvA

• binding phosphoaminophosphonic acid-adenylate ester: F13 (= F32), V18 (= V37), A20 (vs. gap), P39 (= P56), S40 (= S57), G41 (= G58), A42 (≠ C59), G43 (= G60), K44 (= K61), T45 (= T62), T46 (= T63), E166 (= E181)

1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 75% coverage: 23:302/371 of query aligns to 4:285/353 of 1oxuA

• binding adenosine-5'-diphosphate: F13 (= F32), A20 (vs. gap), S40 (= S57), G41 (= G58), A42 (≠ C59), G43 (= G60), K44 (= K61), T45 (= T62), T46 (= T63)

Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
42% identity, 75% coverage: 23:302/371 of query aligns to 4:285/353 of Q97UY8

• S142 (= S157) mutation to A: Decrease in ATPase activity. Can form dimers.
• G144 (= G159) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
• E166 (= E181) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).

1g291 Malk (see paper)
40% identity, 74% coverage: 28:300/371 of query aligns to 9:274/372 of 1g291

• binding magnesium ion: D69 (≠ A88), E71 (vs. gap), K72 (≠ G90), K79 (≠ E97), D80 (≠ K98), Y228 (= Y244), D229 (≠ C245)
• binding pyrophosphate 2-: P37 (= P56), S38 (= S57), G39 (= G58), C40 (= C59), G41 (= G60), K42 (= K61), T43 (= T62), T44 (= T63)

Sites not aligning to the query:

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

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 77% coverage: 20:303/371 of query aligns to 15:304/378 of P69874

• C26 (≠ Q31) mutation to A: Lower ATPase activity and transport efficiency.
• F27 (= F32) mutation to L: Lower ATPase activity and transport efficiency.
• F45 (≠ V50) mutation to L: Lower ATPase activity and transport efficiency.
• C54 (= C59) mutation to T: Loss of ATPase activity and transport.
• L60 (= L65) mutation to F: Lower ATPase activity and transport efficiency.
• L76 (= L81) mutation to P: Lower ATPase activity and transport efficiency.
• V135 (≠ L143) mutation to M: Loss of ATPase activity and transport.
• D172 (= D180) mutation to N: Loss of ATPase activity and transport.
• C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
• E297 (= E296) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to 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)
36% identity, 93% coverage: 25:369/371 of query aligns to 9:344/353 of 1vciA

• binding adenosine-5'-triphosphate: F16 (= F32), F19 (≠ D35), P40 (= P56), S41 (= S57), G42 (= G58), C43 (= C59), G44 (= G60), K45 (= K61), T46 (= T62), T47 (= T63)

P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
41% identity, 71% coverage: 34:296/371 of query aligns to 14:286/369 of P19566

• L86 (= L110) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• P160 (= P182) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
• D165 (= D187) 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)
43% identity, 64% coverage: 22:257/371 of query aligns to 2:234/374 of 2awnB

• binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (= V37), S37 (= S57), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63)

2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
43% identity, 64% coverage: 22:257/371 of query aligns to 2:234/372 of 2awoA

• binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (= V37), S37 (= S57), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63)
• binding magnesium ion: S42 (≠ T62), D157 (= D180)

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
43% identity, 64% coverage: 22:257/371 of query aligns to 3:235/371 of P68187

• A85 (= A109) mutation to M: Suppressor of EAA loop mutations in MalFG.
• K106 (= K130) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V114 (≠ A136) mutation to C: Suppressor of EAA loop mutations in MalFG.
• V117 (≠ L139) mutation to M: Suppressor of EAA loop mutations in MalFG.
• E119 (≠ G141) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• A124 (= A146) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
• G137 (= G159) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
• D158 (= D180) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
• R228 (≠ P250) 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.

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, 64% coverage: 22:257/371 of query aligns to 2:234/371 of 3puyA

• binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F32), V17 (= V37), P36 (= P56), S37 (= S57), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), Q81 (= Q106), R128 (≠ V151), A132 (≠ T155), S134 (= S157), G135 (= G158), G136 (= G159), Q137 (= Q160), E158 (= E181), H191 (= H214)
• binding magnesium ion: S42 (≠ T62), Q81 (= Q106), D157 (= D180)

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
43% identity, 64% coverage: 22:257/371 of query aligns to 2:234/371 of 3puxA

• binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (= V37), S37 (= S57), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), R128 (≠ V151), A132 (≠ T155), L133 (= L156), S134 (= S157), Q137 (= Q160)
• binding beryllium trifluoride ion: S37 (= S57), G38 (= G58), K41 (= K61), Q81 (= Q106), S134 (= S157), G135 (= G158), G136 (= G159), E158 (= E181), H191 (= H214)
• binding magnesium ion: S42 (≠ T62), Q81 (= Q106), D157 (= D180)

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
43% identity, 64% coverage: 22:257/371 of query aligns to 2:234/371 of 3puwA

• binding adenosine-5'-diphosphate: W12 (≠ F32), V17 (= V37), S37 (= S57), G38 (= G58), C39 (= C59), G40 (= G60), K41 (= K61), S42 (≠ T62), T43 (= T63), R128 (≠ V151), A132 (≠ T155), S134 (= S157), Q137 (= Q160)
• binding tetrafluoroaluminate ion: S37 (= S57), G38 (= G58), K41 (= K61), Q81 (= Q106), S134 (= S157), G135 (= G158), G136 (= G159), E158 (= E181), N162 (≠ S185), H191 (= H214)
• binding magnesium ion: S42 (≠ T62), Q81 (= Q106)

3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
38% identity, 89% coverage: 22:351/371 of query aligns to 3:347/350 of 3fvqB