SitesBLAST
Comparing Pf6N2E2_186 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_186 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)
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 95% coverage: 12:251/252 of query aligns to 4:253/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 95% coverage: 12:251/252 of query aligns to 4:253/253 of 1g9xB
1ji0A Crystal structure analysis of the abc transporter from thermotoga maritima
34% identity, 95% coverage: 12:251/252 of query aligns to 6:238/240 of 1ji0A
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 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)
34% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of 1oxuA
Sites not aligning to the query:
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)
34% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of Q97UY8
- S142 (= S155) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G157) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E179) 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+).
5x40A Structure of a cbio dimer bound with amppcp (see paper)
32% identity, 92% coverage: 12:242/252 of query aligns to 4:230/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (= F22), V18 (≠ F25), A20 (= A27), N40 (= N47), G41 (= G48), G43 (= G50), K44 (= K51), S45 (≠ T52), T46 (= T53), Q88 (≠ K92), H139 (≠ D152), M140 (≠ L153), L141 (= L154), S142 (= S155), G144 (= G157), Q145 (= Q158), Q166 (≠ E179), H198 (= H210)
- binding magnesium ion: S45 (≠ T52), Q88 (≠ K92)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 21:225/369 of P19566
- L86 (≠ I98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P180) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (vs. gap) 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 85% coverage: 30:243/252 of query aligns to 21:225/371 of P68187
- A85 (≠ S97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V134) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V137) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R139) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G144) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G157) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D178) 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.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
30% identity, 91% coverage: 15:244/252 of query aligns to 20:240/378 of P69874
- C26 (≠ S21) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F22) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I141) mutation to M: Loss of ATPase activity and transport.
- D172 (= D178) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (≠ N47), G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), Q81 (= Q94), R128 (≠ Q149), A132 (≠ L153), S134 (= S155), G136 (= G157), Q137 (= Q158), E158 (= E179), H191 (= H210)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ Q149), S134 (= S155), Q137 (= Q158)
- binding beryllium trifluoride ion: S37 (≠ N47), G38 (= G48), K41 (= K51), Q81 (= Q94), S134 (= S155), G136 (= G157), H191 (= H210)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ Q149), A132 (≠ L153), S134 (= S155), Q137 (= Q158)
- binding tetrafluoroaluminate ion: S37 (≠ N47), G38 (= G48), K41 (= K51), Q81 (= Q94), S134 (= S155), G135 (≠ H156), G136 (= G157), E158 (= E179), H191 (= H210)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ Q149), A132 (≠ L153), S134 (= S155), Q137 (= Q158)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 20:224/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
34% identity, 85% coverage: 30:243/252 of query aligns to 18:222/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ N47), G36 (= G48), C37 (≠ A49), G38 (= G50), K39 (= K51), S40 (≠ T52), T41 (= T53), R126 (≠ Q149), A130 (≠ L153), S132 (= S155), G134 (= G157), Q135 (= Q158)
Sites not aligning to the query:
6mjpA Lptb(e163q)fgc from vibrio cholerae (see paper)
26% identity, 96% coverage: 11:251/252 of query aligns to 1:235/240 of 6mjpA
3d31A Modbc from methanosarcina acetivorans (see paper)
30% identity, 91% coverage: 15:243/252 of query aligns to 4:219/348 of 3d31A
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
29% identity, 91% coverage: 15:243/252 of query aligns to 9:220/353 of 1vciA
Query Sequence
>Pf6N2E2_186 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_186
MTAVGFQMNKSVLVIEGLTVSFDGFKAVDNLNLYIDRNEVRVVIGPNGAGKTTVLDLICG
KTRATSGSIQFDGKELTKMREYNIVRAGVGRKFQNPSIYENLTVFENLEMSYPAGRKVFG
ALFFKRSAAVIARVEEVAREIFLGELLQQQADLLSHGQKQWLEIGMLLMQDPDLLMLDEP
VAGMSVNERVQTAELLKRISQGRSVLVIEHDMEFVKSIAHKVTVLHQGKVLAEGSMESVQ
NNPKVIEVYLGH
Or try a new SitesBLAST search
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