SitesBLAST
Comparing CCNA_00647 CCNA_00647 nitrate transport ATP-binding protein nrtD 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)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 88% coverage: 7:236/261 of query aligns to 3:229/371 of P68187
- A85 (≠ S88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L124) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (vs. gap) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T130) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G143) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D164) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R235) 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.
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, 88% coverage: 7:236/261 of query aligns to 2:228/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ K17), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q85), R128 (≠ K135), A132 (≠ E139), S134 (= S141), G136 (= G143), Q137 (≠ M144), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 88% coverage: 7:236/261 of query aligns to 2:228/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ K17), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K135), S134 (= S141), Q137 (≠ M144)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S141), G136 (= G143), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 88% coverage: 7:236/261 of query aligns to 2:228/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ K17), V17 (= V24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K135), A132 (≠ E139), S134 (= S141), Q137 (≠ M144)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S141), G135 (= G142), G136 (= G143), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 88% coverage: 7:236/261 of query aligns to 2:228/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ K17), V17 (= V24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K135), A132 (≠ E139), S134 (= S141), Q137 (≠ M144)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 88% coverage: 7:236/261 of query aligns to 2:228/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 80% coverage: 28:236/261 of query aligns to 19:226/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (≠ K135), A130 (≠ E139), S132 (= S141), G134 (= G143), Q135 (≠ M144)
Sites not aligning to the query:
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, 88% coverage: 7:236/261 of query aligns to 3:229/369 of P19566
- L86 (= L89) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P166) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D171) 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.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 75% coverage: 22:216/261 of query aligns to 30:224/378 of P69874
- F45 (= F37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V127) mutation to M: Loss of ATPase activity and transport.
- D172 (= D164) 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)
34% identity, 79% coverage: 17:222/261 of query aligns to 25:245/382 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)
34% identity, 79% coverage: 17:222/261 of query aligns to 25:245/382 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)
34% identity, 79% coverage: 17:222/261 of query aligns to 25:245/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (vs. gap), S61 (= S44), G62 (= G45), G64 (= G47), K65 (= K48), S66 (= S49), T67 (= T50), Q111 (= Q85), K161 (≠ A138), Q162 (≠ E139), S164 (= S141), G166 (= G143), M167 (= M144), Q188 (≠ E165), H221 (= H198)
Sites not aligning to the query:
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, 75% coverage: 28:222/261 of query aligns to 23:217/393 of P9WQI3
- H193 (= H198) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
34% identity, 84% coverage: 4:222/261 of query aligns to 1:214/384 of 8hplC
8hprC Lpqy-sugabc in state 4 (see paper)
36% identity, 74% coverage: 30:222/261 of query aligns to 24:216/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q85), Q133 (≠ E139), G136 (= G142), G137 (= G143), Q138 (≠ M144), H192 (= H198)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
36% identity, 74% coverage: 30:222/261 of query aligns to 24:216/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q85), R129 (≠ K135), Q133 (≠ E139), S135 (= S141), G136 (= G142), G137 (= G143), Q159 (≠ E165), H192 (= H198)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 80% coverage: 28:236/261 of query aligns to 14:198/344 of 2awnC
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
37% identity, 76% coverage: 25:223/261 of query aligns to 16:211/348 of 3d31A
Sites not aligning to the query:
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
37% identity, 80% coverage: 3:212/261 of query aligns to 1:215/226 of 5xu1B
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
35% identity, 81% coverage: 6:216/261 of query aligns to 2:221/232 of 1f3oA
Query Sequence
>CCNA_00647 CCNA_00647 nitrate transport ATP-binding protein nrtD
MAKAYLSIENVGVTFAKGSVRSEVLTGVDLKIDKGEFVSIIGHSGCGKSTLLNVVAGLVP
VTTGAVILDRQEVNAPGPDRAVVFQNHSLLPWLSVRENVSLAVDKVFGGVKSAAERKEWV
LHNLELVKMTHALDKRPAEISGGMKQRVGIARALSMEPKVLLLDEPFGALDALTRAHLQD
SVMEIHSALKNTVLMITHDVDEATLLSDRIVMMTNGPRACVGQVLDVPLARPRDRLAVAE
HPTYVHARAAVIEFLYARRAA
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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