SitesBLAST
Comparing 8499757 FitnessBrowser__Miya:8499757 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 92% coverage: 1:229/249 of query aligns to 17:235/378 of P69874
- C26 (≠ T10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F34) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S43) mutation to T: Loss of ATPase activity and transport.
- L60 (= L49) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L65) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) 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, 86% coverage: 2:215/249 of query aligns to 4:212/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D165) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
36% identity, 81% coverage: 10:211/249 of query aligns to 21:241/382 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)
36% identity, 81% coverage: 10:211/249 of query aligns to 21:241/382 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
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
39% identity, 87% coverage: 2:218/249 of query aligns to 3:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F11), S37 (≠ G41), G38 (≠ Q42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), Q81 (= Q82), R128 (≠ H129), A132 (≠ Q133), S134 (= S135), G136 (= G137), Q137 (≠ M138), E158 (= E159), H191 (≠ N192)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 87% coverage: 2:218/249 of query aligns to 3:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F11), G38 (≠ Q42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (≠ H129), S134 (= S135), Q137 (≠ M138)
- binding beryllium trifluoride ion: S37 (≠ G41), G38 (≠ Q42), K41 (= K45), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (≠ N192)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 87% coverage: 2:218/249 of query aligns to 3:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (= V21), G38 (≠ Q42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (≠ H129), A132 (≠ Q133), S134 (= S135), Q137 (≠ M138)
- binding tetrafluoroaluminate ion: S37 (≠ G41), G38 (≠ Q42), K41 (= K45), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (≠ N192)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 87% coverage: 2:218/249 of query aligns to 3:214/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (= V21), G38 (≠ Q42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (≠ H129), A132 (≠ Q133), S134 (= S135), Q137 (≠ M138)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 87% coverage: 2:218/249 of query aligns to 3:214/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 87% coverage: 2:218/249 of query aligns to 4:215/371 of P68187
- A85 (≠ M85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ Y117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) 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)
39% identity, 87% coverage: 2:218/249 of query aligns to 1:212/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F11), S35 (≠ G41), G36 (≠ Q42), C37 (≠ S43), G38 (= G44), K39 (= K45), S40 (= S46), T41 (= T47), R126 (≠ H129), A130 (≠ Q133), S132 (= S135), G134 (= G137), Q135 (≠ M138)
7ahdC Opua (e190q) occluded (see paper)
35% identity, 81% coverage: 10:211/249 of query aligns to 21:241/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (vs. gap), S61 (≠ G41), G62 (≠ Q42), G64 (= G44), K65 (= K45), S66 (= S46), T67 (= T47), Q111 (= Q82), K161 (≠ H132), Q162 (= Q133), S164 (= S135), G166 (= G137), M167 (= M138), Q188 (≠ E159), H221 (≠ N192)
Sites not aligning to the query:
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
39% identity, 87% coverage: 1:217/249 of query aligns to 1:225/232 of 1f3oA
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
37% identity, 84% coverage: 1:209/249 of query aligns to 3:218/226 of 5xu1B
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
39% identity, 87% coverage: 1:217/249 of query aligns to 1:225/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F11), S40 (≠ G41), G41 (≠ Q42), S42 (= S43), G43 (= G44), K44 (= K45), S45 (= S46), T46 (= T47), F138 (= F126), Q145 (= Q133), S147 (= S135), G149 (= G137), Q150 (≠ M138), H204 (≠ N192)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
35% identity, 89% coverage: 1:222/249 of query aligns to 1:228/375 of 2d62A
1g291 Malk (see paper)
36% identity, 76% coverage: 18:207/249 of query aligns to 15:213/372 of 1g291
- binding magnesium ion: D69 (≠ G72), E71 (vs. gap), K72 (vs. gap), K79 (vs. gap), D80 (≠ G74)
- binding pyrophosphate 2-: S38 (≠ G41), G39 (≠ Q42), C40 (≠ S43), G41 (= G44), K42 (= K45), T43 (≠ S46), T44 (= T47)
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 85% coverage: 1:211/249 of query aligns to 1:206/348 of 3d31A
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 81% coverage: 17:218/249 of query aligns to 6:184/344 of 2awnC
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
36% identity, 84% coverage: 1:209/249 of query aligns to 1:216/343 of P30750
- 40:46 (vs. 41:47, 57% identical) binding
- E166 (= E159) 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
>8499757 FitnessBrowser__Miya:8499757
MIECRNVSKTFIQKGKQEVPVLEDVSLDVQANEFVVILGPGQSGKSTLLRIIAGLETPTT
GTVTLDGEPVTGPGADRGLVFQGYMLFPWKTVLGNVEMGPKLCGLPGDEARDIALHYIDL
VGLKGFEKHYPHQLSGGMKQRVGIARAYANKPRVMLLDEPFGQLDAQTRIFMEQETERIW
QTDKRTVLFVTNNTDEALFLADRIVTIEGKLPGRVQRTYTVDLPRPRDLTGKHFLEMRRE
IIDASVLTL
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