SitesBLAST
Comparing AO353_02425 FitnessBrowser__pseudo3_N2E3:AO353_02425 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)
52% identity, 77% coverage: 20:277/334 of query aligns to 29:286/378 of P69874
- F45 (= F36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ E267) mutation to A: Lower ATPase activity and transport efficiency.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
46% identity, 74% coverage: 1:248/334 of query aligns to 4:254/375 of 2d62A
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)
44% identity, 80% coverage: 1:267/334 of query aligns to 1:264/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1g291 Malk (see paper)
49% identity, 66% coverage: 26:247/334 of query aligns to 21:250/372 of 1g291
- binding magnesium ion: D69 (= D68), E71 (≠ H70), K72 (≠ D71), K79 (≠ Q78), D80 (≠ K79)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (≠ S48), T44 (= T49)
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)
45% identity, 72% coverage: 1:241/334 of query aligns to 1:236/371 of P68187
- A85 (= A90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ N111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ V233) 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
45% identity, 72% coverage: 1:241/334 of query aligns to 1:236/369 of P19566
- L86 (= L91) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) 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)
45% identity, 71% coverage: 4:241/334 of query aligns to 3:235/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
45% identity, 71% coverage: 4:241/334 of query aligns to 3:235/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), Q81 (= Q87), R128 (= R134), A132 (≠ Q138), S134 (= S140), G136 (= G142), Q137 (= Q143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
45% identity, 71% coverage: 4:241/334 of query aligns to 3:235/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (= R134), S134 (= S140), Q137 (= Q143)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
45% identity, 71% coverage: 4:241/334 of query aligns to 3:235/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (= R134), A132 (≠ Q138), S134 (= S140), Q137 (= Q143)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
45% identity, 71% coverage: 4:241/334 of query aligns to 3:235/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (= R134), A132 (≠ Q138), S134 (= S140), Q137 (= Q143)
- binding magnesium ion: S42 (= S48), Q81 (= Q87)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
45% identity, 71% coverage: 4:241/334 of query aligns to 1:233/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (= S48), T41 (= T49), R126 (= R134), A130 (≠ Q138), S132 (= S140), G134 (= G142), Q135 (= Q143)
8hprD Lpqy-sugabc in state 4 (see paper)
38% identity, 98% coverage: 4:331/334 of query aligns to 3:349/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S43), C40 (= C45), G41 (= G46), K42 (= K47), S43 (= S48), T44 (= T49), Q82 (= Q87), R129 (= R134), Q133 (= Q138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (= S48), Q82 (= Q87)
8hprC Lpqy-sugabc in state 4 (see paper)
38% identity, 98% coverage: 4:331/334 of query aligns to 3:350/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (= S48), Q82 (= Q87), Q133 (= Q138), G136 (= G141), G137 (= G142), Q138 (= Q143), H192 (= H197)
- binding magnesium ion: S43 (= S48), Q82 (= Q87)
8hplC Lpqy-sugabc in state 1 (see paper)
39% identity, 83% coverage: 4:281/334 of query aligns to 3:276/384 of 8hplC
3d31A Modbc from methanosarcina acetivorans (see paper)
38% identity, 87% coverage: 24:315/334 of query aligns to 16:328/348 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)
44% identity, 76% coverage: 1:255/334 of query aligns to 4:247/353 of 1vciA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 6:274/334 of query aligns to 2:286/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 6:274/334 of query aligns to 2:286/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 81% coverage: 6:274/334 of query aligns to 2:286/353 of 1oxuA
Query Sequence
>AO353_02425 FitnessBrowser__pseudo3_N2E3:AO353_02425
MSYVSVQHLQKSYSQTGSAGTPVFSDINCEIQKGEFVTLLGPSGCGKSTLLRCIAGLTAV
DGGKILLDGHDLVPLSPQKRGIGMVFQSYALFPNMTVEQNVAFGLRMQKVNADDSRKRVL
QVLQLVELTDFASRYPHQLSGGQCQRVALARSLVTRPRLLLLDEPLSALDARIRKHLREQ
IRQIQRELGLTTIFVTHDQEEALTMSDRIFLMNQGKIVQSGDAETLYTAPVDVFAAGFIG
NYNLLDAASASKLLQRPINGRIAIRPEAIELSRNGEPDALIRSHSLLGNVIRYRVEARGV
ELVVDVLNRSAADLHADGQRLALSIDPTALCEVA
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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