SitesBLAST
Comparing Synpcc7942_0960 Synpcc7942_0960 ATPase 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)
1g291 Malk (see paper)
52% identity, 89% coverage: 45:414/417 of query aligns to 14:371/372 of 1g291
- binding magnesium ion: D69 (≠ R100), E71 (vs. gap), K72 (vs. gap), K79 (= K104), D80 (≠ A105), E292 (= E339), D293 (≠ H340), K359 (≠ Q402)
- binding pyrophosphate 2-: S38 (= S69), G39 (= G70), C40 (= C71), G41 (= G72), K42 (= K73), T43 (≠ S74), T44 (= T75)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
48% identity, 89% coverage: 45:414/417 of query aligns to 17:374/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
46% identity, 93% coverage: 26:414/417 of query aligns to 7:352/353 of 1vciA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
46% identity, 89% coverage: 45:415/417 of query aligns to 13:362/374 of 2awnB
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)
46% identity, 89% coverage: 45:415/417 of query aligns to 14:361/369 of P19566
- L86 (= L117) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P215) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D220) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E359) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
46% identity, 89% coverage: 45:415/417 of query aligns to 13:362/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S69), G38 (= G70), C39 (= C71), G40 (= G72), K41 (= K73), S42 (= S74), T43 (= T75), Q81 (= Q113), R128 (= R184), A132 (≠ Q188), S134 (= S190), G136 (= G192), Q137 (= Q193), E158 (= E214), H191 (= H247)
- binding magnesium ion: S42 (= S74), Q81 (= Q113)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
46% identity, 89% coverage: 45:415/417 of query aligns to 13:362/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G70), C39 (= C71), G40 (= G72), K41 (= K73), S42 (= S74), T43 (= T75), R128 (= R184), S134 (= S190), Q137 (= Q193)
- binding beryllium trifluoride ion: S37 (= S69), G38 (= G70), K41 (= K73), Q81 (= Q113), S134 (= S190), G136 (= G192), H191 (= H247)
- binding magnesium ion: S42 (= S74), Q81 (= Q113)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
46% identity, 89% coverage: 45:415/417 of query aligns to 13:362/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (= V49), G38 (= G70), C39 (= C71), G40 (= G72), K41 (= K73), S42 (= S74), T43 (= T75), R128 (= R184), A132 (≠ Q188), S134 (= S190), Q137 (= Q193)
- binding tetrafluoroaluminate ion: S37 (= S69), G38 (= G70), K41 (= K73), Q81 (= Q113), S134 (= S190), G135 (= G191), G136 (= G192), E158 (= E214), H191 (= H247)
- binding magnesium ion: S42 (= S74), Q81 (= Q113)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
46% identity, 89% coverage: 45:415/417 of query aligns to 13:362/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (= V49), G38 (= G70), C39 (= C71), G40 (= G72), K41 (= K73), S42 (= S74), T43 (= T75), R128 (= R184), A132 (≠ Q188), S134 (= S190), Q137 (= Q193)
- binding magnesium ion: S42 (= S74), Q81 (= Q113)
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)
46% identity, 89% coverage: 45:415/417 of query aligns to 14:363/371 of P68187
- A85 (= A116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R137) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V169) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V172) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ T174) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D179) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G192) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D213) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R283) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L296) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W320) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G329) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ E333) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G335) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ I353) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E359) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ E373) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G391) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ T397) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F406) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
46% identity, 89% coverage: 45:415/417 of query aligns to 11:360/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S69), G36 (= G70), C37 (= C71), G38 (= G72), K39 (= K73), S40 (= S74), T41 (= T75), R126 (= R184), A130 (≠ Q188), S132 (= S190), G134 (= G192), Q135 (= Q193)
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)
41% identity, 93% coverage: 23:411/417 of query aligns to 1:384/393 of P9WQI3
- H193 (= H247) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 93% coverage: 24:411/417 of query aligns to 1:356/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F35), S38 (= S69), C40 (= C71), G41 (= G72), K42 (= K73), S43 (= S74), T44 (= T75), Q82 (= Q113), R129 (= R184), Q133 (= Q188), S135 (= S190), G136 (= G191), G137 (= G192), Q159 (≠ E214), H192 (= H247)
- binding magnesium ion: S43 (= S74), Q82 (= Q113)
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 93% coverage: 24:411/417 of query aligns to 1:357/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F35), S38 (= S69), G39 (= G70), G41 (= G72), K42 (= K73), S43 (= S74), Q82 (= Q113), Q133 (= Q188), G136 (= G191), G137 (= G192), Q138 (= Q193), H192 (= H247)
- binding magnesium ion: S43 (= S74), Q82 (= Q113)
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 93% coverage: 24:411/417 of query aligns to 1:378/384 of 8hplC
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 90% coverage: 41:415/417 of query aligns to 2:332/344 of 2awnC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 72% coverage: 49:350/417 of query aligns to 32:308/378 of P69874
- F45 (= F62) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C71) mutation to T: Loss of ATPase activity and transport.
- L60 (= L77) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V93) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L176) mutation to M: Loss of ATPase activity and transport.
- D172 (= D213) mutation to N: Loss of ATPase activity and transport.
- C276 (= C314) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E339) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: 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.
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 89% coverage: 45:415/417 of query aligns to 13:320/330 of 2awnA
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 59% coverage: 43:290/417 of query aligns to 14:242/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 59% coverage: 43:290/417 of query aligns to 14:242/353 of 1oxvA
Sites not aligning to the query:
Query Sequence
>Synpcc7942_0960 Synpcc7942_0960 ATPase
LPRSAARVTSAKLFPTFGRDCNVAGVVFEEIEKRFPEQARSPQKGEVVVLNGINLEIADG
EFMVVVGPSGCGKSTLLRLLAGLETPSRGLIKVGDRRVDRLPAKARDIAMVFQSYALYPH
LSVYDNLAFGLRRQGDRPWWQQQLALATRSLPKSLQYEPEQEARIKRRVREVATMLQLDT
LLDRQPKQLSGGQKQRVALGRAIARNPQVFLMDEPLSNLDAKLRAETRAQIVSLQRQLGV
TTLYVTHDQTEAMTMGDRIAVLNRGHLQQVASPLEIYDRPANRFVAQFIGSPPMNLIPVT
VRAPLQLTTENFRCTLPEAWEPVLRLYDGQTVELGIRPEHLEVGAAASKNLLITVTGVEA
LGSDTFIAGELKESGIAVQARLAPQQCWQMGDRLWLTFKPDQIHLFDLETGKAIRPS
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