SitesBLAST
Comparing Dsui_1833 Dsui_1833 nitrate transport ATP-binding subunits C and D 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
39% identity, 79% coverage: 17:225/266 of query aligns to 35:252/382 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)
39% identity, 79% coverage: 17:225/266 of query aligns to 35:252/382 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)
38% identity, 79% coverage: 17:225/266 of query aligns to 35:252/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ F21), S61 (= S43), G62 (= G44), G64 (= G46), K65 (= K47), S66 (= S48), T67 (= T49), Q111 (= Q84), K161 (≠ H137), Q162 (≠ E138), S164 (= S140), G166 (= G142), M167 (= M143), Q188 (≠ E164), H221 (= H197)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 76% coverage: 19:221/266 of query aligns to 17:225/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 80% coverage: 4:215/266 of query aligns to 17:224/378 of P69874
- C26 (≠ T13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F14) mutation to L: Lower ATPase activity and transport efficiency.
- 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 (≠ C67) 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.
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.
1g291 Malk (see paper)
36% identity, 76% coverage: 19:221/266 of query aligns to 14:222/372 of 1g291
- binding magnesium ion: D69 (≠ G74), E71 (= E78), K72 (≠ R79), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (≠ S48), T44 (= T49)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 83% coverage: 5:226/266 of query aligns to 3:220/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 83% coverage: 5:226/266 of query aligns to 4:221/371 of P68187
- A85 (≠ S87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ T119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A124) 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.
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.
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, 83% coverage: 5:226/266 of query aligns to 3:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F14), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), Q81 (= Q84), R128 (≠ K134), A132 (≠ E138), S134 (= S140), G136 (= G142), Q137 (≠ M143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 83% coverage: 5:226/266 of query aligns to 3:220/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F14), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ K134), S134 (= S140), Q137 (≠ M143)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q84), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 83% coverage: 5:226/266 of query aligns to 3:220/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ K134), A132 (≠ E138), S134 (= S140), Q137 (≠ M143)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q84), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 83% coverage: 5:226/266 of query aligns to 3:220/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A23), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), R128 (≠ K134), A132 (≠ E138), S134 (= S140), Q137 (≠ M143)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 83% coverage: 5:226/266 of query aligns to 1:218/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F14), S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (= S48), T41 (= T49), R126 (≠ K134), A130 (≠ E138), S132 (= S140), G134 (= G142), Q135 (≠ M143)
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)
39% identity, 75% coverage: 23:221/266 of query aligns to 19:217/393 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
39% identity, 78% coverage: 19:226/266 of query aligns to 14:221/369 of P19566
- L86 (= L88) 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 7:222/266 of query aligns to 6:224/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 7:222/266 of query aligns to 6:224/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 81% coverage: 7:222/266 of query aligns to 6:224/353 of 1oxuA
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)
35% identity, 81% coverage: 7:222/266 of query aligns to 6:224/353 of Q97UY8
- S142 (= S140) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G142) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E164) 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+).
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
35% identity, 86% coverage: 5:233/266 of query aligns to 7:222/353 of 1vciA
Query Sequence
>Dsui_1833 Dsui_1833 nitrate transport ATP-binding subunits C and D
MEKFVQIEAVGQTFDTKKGKFVALRDVDLSIRQGEFIALIGHSGCGKSTLLNLIAGLTRP
TDGALICDGREIAGPGPERGVVFQNHSLLPWLTCFDNVYLAVERVFAAKEGKAKLKQRTH
DALALVGLTHAETKFPHEISGGMKQRVGIARALSMQPKVLLMDEPFGALDALTRAKLQDE
LMKICDATQATVVMVTHDVDEAVLLSDRIVMMTNGPAATIGEILSVDLPRPRNRLALAND
PKYIAARAAVLEFLYEKQAHKEVLAA
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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