SitesBLAST
Comparing AO353_11720 FitnessBrowser__pseudo3_N2E3:AO353_11720 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
39% identity, 66% coverage: 23:197/264 of query aligns to 44:227/382 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)
39% identity, 66% coverage: 23:197/264 of query aligns to 44:227/382 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)
39% identity, 66% coverage: 23:197/264 of query aligns to 44:227/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S40), G62 (= G41), G64 (= G43), K65 (= K44), S66 (≠ T45), T67 (≠ S46), Q111 (= Q81), K161 (≠ W131), Q162 (= Q132), S164 (= S134), G166 (= G136), M167 (≠ Q137), Q188 (≠ E158), H221 (= H191)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 77% coverage: 3:206/264 of query aligns to 17:221/378 of P69874
- C26 (≠ Q12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V120) mutation to M: Loss of ATPase activity and transport.
- D172 (= D157) 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)
37% identity, 78% coverage: 1:206/264 of query aligns to 1:207/369 of P19566
- L86 (= L85) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P159) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D164) 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.
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 78% coverage: 1:206/264 of query aligns to 1:208/393 of P9WQI3
- H193 (= H191) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 73% coverage: 21:213/264 of query aligns to 22:221/375 of 2d62A
3d31A Modbc from methanosarcina acetivorans (see paper)
37% identity, 75% coverage: 3:200/264 of query aligns to 1:195/348 of 3d31A
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 78% coverage: 1:206/264 of query aligns to 1:207/371 of P68187
- A85 (= A84) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A118) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A123) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G136) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D157) 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.
8hplC Lpqy-sugabc in state 1 (see paper)
34% identity, 78% coverage: 2:206/264 of query aligns to 1:205/384 of 8hplC
8hprC Lpqy-sugabc in state 4 (see paper)
34% identity, 78% coverage: 2:206/264 of query aligns to 1:207/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (≠ T45), Q82 (= Q81), Q133 (= Q132), G136 (= G135), G137 (= G136), Q138 (= Q137), H192 (= H191)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q81)
8hprD Lpqy-sugabc in state 4 (see paper)
34% identity, 78% coverage: 2:206/264 of query aligns to 1:207/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S40), C40 (≠ S42), G41 (= G43), K42 (= K44), S43 (≠ T45), T44 (≠ S46), Q82 (= Q81), R129 (= R128), Q133 (= Q132), S135 (= S134), G136 (= G135), G137 (= G136), Q159 (≠ E158), H192 (= H191)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q81)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 71% coverage: 20:206/264 of query aligns to 17:206/374 of 2awnB
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)
38% identity, 71% coverage: 20:206/264 of query aligns to 17:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S40), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (≠ S46), Q81 (= Q81), R128 (= R128), A132 (≠ Q132), S134 (= S134), G136 (= G136), Q137 (= Q137), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q81)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 71% coverage: 20:206/264 of query aligns to 17:206/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (≠ S46), R128 (= R128), S134 (= S134), Q137 (= Q137)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q81), S134 (= S134), G136 (= G136), H191 (= H191)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q81)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 71% coverage: 20:206/264 of query aligns to 17:206/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V20), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (≠ S46), R128 (= R128), A132 (≠ Q132), S134 (= S134), Q137 (= Q137)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q81), S134 (= S134), G135 (= G135), G136 (= G136), E158 (= E158), H191 (= H191)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q81)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 71% coverage: 20:206/264 of query aligns to 17:206/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V20), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (≠ S46), R128 (= R128), A132 (≠ Q132), S134 (= S134), Q137 (= Q137)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q81)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 71% coverage: 20:206/264 of query aligns to 15:204/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S40), G36 (= G41), C37 (≠ S42), G38 (= G43), K39 (= K44), S40 (≠ T45), T41 (≠ S46), R126 (= R128), A130 (≠ Q132), S132 (= S134), G134 (= G136), Q135 (= Q137)
Sites not aligning to the query:
1g291 Malk (see paper)
40% identity, 67% coverage: 23:200/264 of query aligns to 21:207/372 of 1g291
- binding magnesium ion: D69 (≠ V67), E71 (≠ V69), K72 (= K70), K79 (≠ A74), D80 (≠ E75)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (≠ S42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (≠ S46)
Sites not aligning to the query:
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
36% identity, 70% coverage: 20:205/264 of query aligns to 22:215/226 of 5xu1B
Query Sequence
>AO353_11720 FitnessBrowser__pseudo3_N2E3:AO353_11720
MALLQLERISAQYPGTAEPVLADISLSLGPQQLLVALGPSGSGKTSLLNLIAGFVEPSAG
RITLDGVPVKGPSAERGVVFQDDALLPWQDVLANVGFGLELAGVPRDKREVRAREMLALV
DLAGFDARRIWQLSGGQKQRVGLARALAADPRVLLMDEPFGALDAFTREQMQELLLQVWR
RTAKPVFLITHDIEEAVFLATDLILLAPNPGQIVERLLLDFGQRYAAGESARAIKSDPRF
IETREHVLARVFSQRNAAQRQERA
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