SitesBLAST
Comparing Synpcc7942_0947 Synpcc7942_0947 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)
44% identity, 94% coverage: 18:352/355 of query aligns to 15:368/372 of 1g291
- binding magnesium ion: D69 (≠ T72), E71 (vs. gap), K72 (vs. gap), K79 (≠ G76), D80 (= D77), E292 (= E280), D293 (≠ H281), K359 (≠ S343)
- binding pyrophosphate 2-: S38 (= S41), G39 (= G42), C40 (= C43), G41 (= G44), K42 (= K45), T43 (≠ S46), T44 (= T47)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 82% coverage: 18:309/355 of query aligns to 18:329/375 of 2d62A
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 78% coverage: 8:283/355 of query aligns to 5:287/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y15), S38 (= S41), G39 (= G42), G41 (= G44), K42 (= K45), S43 (= S46), Q82 (= Q85), Q133 (= Q136), G136 (= G139), G137 (= G140), Q138 (= Q141), H192 (= H195)
- binding magnesium ion: S43 (= S46), Q82 (= Q85)
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 78% coverage: 8:283/355 of query aligns to 5:287/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y15), S38 (= S41), C40 (= C43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (= T47), Q82 (= Q85), R129 (= R132), Q133 (= Q136), S135 (= S138), G136 (= G139), G137 (= G140), Q159 (≠ E162), H192 (= H195)
- binding magnesium ion: S43 (= S46), Q82 (= Q85)
8hplC Lpqy-sugabc in state 1 (see paper)
48% identity, 78% coverage: 8:283/355 of query aligns to 5:285/384 of 8hplC
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 97% coverage: 5:347/355 of query aligns to 2:354/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 97% coverage: 5:347/355 of query aligns to 3:355/371 of P68187
- A85 (= A88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ H122) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D127) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D161) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ A231) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L244) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (vs. gap) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ R270) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ L274) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G276) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ V295) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E301) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ E318) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (≠ Q336) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (vs. gap) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F347) mutation to 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)
41% identity, 97% coverage: 5:347/355 of query aligns to 2:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y15), S37 (= S41), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), Q81 (= Q85), R128 (= R132), A132 (≠ Q136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
41% identity, 97% coverage: 5:347/355 of query aligns to 2:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (= R132), S134 (= S138), Q137 (= Q141)
- binding beryllium trifluoride ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q85), S134 (= S138), G136 (= G140), H191 (= H195)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
41% identity, 97% coverage: 5:347/355 of query aligns to 2:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (= V20), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (= R132), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding tetrafluoroaluminate ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q85), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
41% identity, 97% coverage: 5:347/355 of query aligns to 2:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (= V20), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (= R132), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 96% coverage: 6:347/355 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y15), S35 (= S41), G36 (= G42), C37 (= C43), G38 (= G44), K39 (= K45), S40 (= S46), T41 (= T47), R126 (= R132), A130 (≠ Q136), S132 (= S138), G134 (= G140), Q135 (= Q141)
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)
45% identity, 85% coverage: 8:309/355 of query aligns to 6:320/393 of P9WQI3
- H193 (= H195) 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)
41% identity, 97% coverage: 5:347/355 of query aligns to 3:353/369 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 (= P163) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D168) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E301) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 97% coverage: 6:351/355 of query aligns to 7:348/353 of 1vciA
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 91% coverage: 24:347/355 of query aligns to 13:324/344 of 2awnC
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)
48% identity, 67% coverage: 6:242/355 of query aligns to 18:253/378 of P69874
- C26 (≠ A14) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y15) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F34) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C43) mutation to T: Loss of ATPase activity and transport.
- L60 (= L49) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L65) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) 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.
3d31A Modbc from methanosarcina acetivorans (see paper)
39% identity, 76% coverage: 24:293/355 of query aligns to 18:287/348 of 3d31A
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 78% coverage: 8:285/355 of query aligns to 6:284/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 78% coverage: 8:285/355 of query aligns to 6:284/353 of 1oxvA
Query Sequence
>Synpcc7942_0947 Synpcc7942_0947 ATPase
MASFALELRQLRKAYSPSVVPVANLSLQLQPGEFLTLLGPSGCGKSTTLRLIAGLDQPTS
GSIWLGDREITTLPPGDRDMAMVFQSYALYPHLNVRQNLTLGLQIRRTSAAEIEQRLQQV
AHNLELDHLLDRRPAQLSGGQRQRVALGRALVRQPSVFLLDEPLSNLDALLREQVRAQMK
ALFSQQASPVVYVTHDQTEALSLSHRIAILNGGHLQQLDSPDRIYQAPANAFVAGFIGSP
RMNLLPLPIHSGQAWLGSRALPIPSHLAARSQVLWGLRPEHLKLATPEVERAIPVQLHLT
ENLGMQRLLTVAIAANPEVRLRLLMPSDQPIPTDLQVTFEPESQHWFCPSTGDRL
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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