SitesBLAST
Comparing SM_b20569 FitnessBrowser__Smeli:SM_b20569 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)
43% identity, 77% coverage: 30:227/256 of query aligns to 32:235/378 of P69874
- F45 (≠ C43) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S52) mutation to T: Loss of ATPase activity and transport.
- L60 (= L58) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V130) mutation to M: Loss of ATPase activity and transport.
- D172 (= D167) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
43% identity, 73% coverage: 35:222/256 of query aligns to 46:239/382 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, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
43% identity, 73% coverage: 35:222/256 of query aligns to 46:239/382 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)
42% identity, 73% coverage: 35:222/256 of query aligns to 46:239/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S50), G62 (= G51), G64 (= G53), K65 (= K54), S66 (≠ T55), T67 (= T56), Q111 (= Q91), K161 (= K141), Q162 (= Q142), S164 (= S144), G166 (= G146), M167 (= M147), Q188 (≠ E168), H221 (= H201)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 85% coverage: 10:227/256 of query aligns to 5:230/375 of 2d62A
1g291 Malk (see paper)
38% identity, 77% coverage: 28:224/256 of query aligns to 16:224/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (vs. gap), D80 (≠ G83)
- binding pyrophosphate 2-: S38 (= S50), G39 (= G51), C40 (≠ S52), G41 (= G53), K42 (= K54), T43 (= T55), T44 (= T56)
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)
40% identity, 81% coverage: 10:216/256 of query aligns to 1:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F21), S37 (= S50), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), Q81 (= Q91), R128 (≠ A138), A132 (≠ Q142), S134 (= S144), G136 (= G146), Q137 (≠ M147), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 81% coverage: 10:216/256 of query aligns to 1:206/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F21), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ A138), S134 (= S144), Q137 (≠ M147)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q91), S134 (= S144), G136 (= G146), H191 (= H201)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 81% coverage: 10:216/256 of query aligns to 1:206/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F21), V17 (= V30), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ A138), A132 (≠ Q142), S134 (= S144), Q137 (≠ M147)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q91), S134 (= S144), G135 (= G145), G136 (= G146), E158 (= E168), H191 (= H201)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q91)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 81% coverage: 10:216/256 of query aligns to 1:206/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F21), V17 (= V30), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (≠ A138), A132 (≠ Q142), S134 (= S144), Q137 (≠ M147)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q91)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 81% coverage: 10:216/256 of query aligns to 1:206/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 81% coverage: 10:216/256 of query aligns to 2:207/371 of P68187
- A85 (≠ R94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A123) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ Y126) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ S128) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A133) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G146) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D167) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 80% coverage: 12:216/256 of query aligns to 1:204/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F21), S35 (= S50), G36 (= G51), C37 (≠ S52), G38 (= G53), K39 (= K54), S40 (≠ T55), T41 (= T56), R126 (≠ A138), A130 (≠ Q142), S132 (= S144), G134 (= G146), Q135 (≠ M147)
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, 80% coverage: 12:216/256 of query aligns to 4:207/369 of P19566
- L86 (= L95) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P169) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D174) 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.
3c4jA Abc protein artp in complex with atp-gamma-s
40% identity, 80% coverage: 12:216/256 of query aligns to 4:211/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
40% identity, 80% coverage: 12:216/256 of query aligns to 4:211/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
40% identity, 80% coverage: 12:216/256 of query aligns to 4:211/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
40% identity, 80% coverage: 12:216/256 of query aligns to 4:211/242 of 2oljA
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
36% identity, 91% coverage: 11:243/256 of query aligns to 6:229/353 of 1vciA
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
36% identity, 80% coverage: 12:216/256 of query aligns to 2:214/343 of P30750
- 40:46 (vs. 50:56, 71% identical) binding
- E166 (= E168) 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
Query Sequence
>SM_b20569 FitnessBrowser__Smeli:SM_b20569
MAEVRSLRRGEVALRDLSKSFQINGRPLSVLRNLNLDIRSGECLAIVGASGSGKTTLLRV
LAGLETADAGRVLIDGRPVAGVGRERAVIFQEPRLLPWLTVLGNVAFGLKVRGEDSGRAE
QRARHYISLVGLADFQDAYPKQLSGGMAQRVGLARALTVKPEILLLDEPLGALDAMTKLT
MQQELERIWREENVTMVLVTHDLEEAIYLADRVLILPKQKDGAPRAIDIDLPRPRDRSGA
RFVRYRQELLREFGLH
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