SitesBLAST
Comparing SM_b20630 FitnessBrowser__Smeli:SM_b20630 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)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
50% identity, 98% coverage: 9:361/361 of query aligns to 2:362/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
50% identity, 98% coverage: 9:361/361 of query aligns to 3:363/371 of P68187
- A85 (= A91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D130) 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 (≠ M234) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F247) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ E266) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G277) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ L281) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G283) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ A301) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E307) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ D321) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G338) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ A344) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F353) 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)
50% identity, 98% coverage: 9:361/361 of query aligns to 2:362/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y19), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q88), R128 (= R135), A132 (≠ Q139), S134 (= S141), G136 (= G143), Q137 (= Q144), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
50% identity, 98% coverage: 9:361/361 of query aligns to 2:362/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (= R135), S134 (= S141), Q137 (= Q144)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (= S141), G136 (= G143), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
50% identity, 98% coverage: 9:361/361 of query aligns to 2:362/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), V17 (= V24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (= R135), A132 (≠ Q139), S134 (= S141), Q137 (= Q144)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (= S141), G135 (= G142), G136 (= G143), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
50% identity, 98% coverage: 9:361/361 of query aligns to 2:362/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), V17 (= V24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (= R135), A132 (≠ Q139), S134 (= S141), Q137 (= Q144)
- binding magnesium ion: S42 (= S49), Q81 (= Q88)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
49% identity, 98% coverage: 10:361/361 of query aligns to 1:360/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y19), S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (= R135), A130 (≠ Q139), S132 (= S141), G134 (= G143), Q135 (= Q144)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
49% identity, 98% coverage: 9:361/361 of query aligns to 3:361/369 of P19566
- L86 (= L92) 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.
- E306 (= E307) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
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)
53% identity, 86% coverage: 10:320/361 of query aligns to 4:325/393 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.
8hprC Lpqy-sugabc in state 4 (see paper)
48% identity, 95% coverage: 10:353/361 of query aligns to 3:352/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y19), S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q88), Q133 (= Q139), G136 (= G142), G137 (= G143), Q138 (= Q144), H192 (= H198)
- binding magnesium ion: S43 (= S49), Q82 (= Q88)
8hplC Lpqy-sugabc in state 1 (see paper)
52% identity, 86% coverage: 10:320/361 of query aligns to 3:322/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 95% coverage: 10:353/361 of query aligns to 3:351/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y19), S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q88), R129 (= R135), Q133 (= Q139), S135 (= S141), G136 (= G142), G137 (= G143), Q159 (≠ E165), H192 (= H198)
- binding magnesium ion: S43 (= S49), Q82 (= Q88)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
49% identity, 93% coverage: 28:361/361 of query aligns to 14:332/344 of 2awnC
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
48% identity, 87% coverage: 5:318/361 of query aligns to 2:332/375 of 2d62A
1g291 Malk (see paper)
51% identity, 84% coverage: 10:313/361 of query aligns to 4:324/372 of 1g291
- binding magnesium ion: D69 (= D75), E71 (vs. gap), K72 (vs. gap), K79 (≠ S79), D80 (≠ E80), E292 (= E287), D293 (≠ H288)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50)
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)
45% identity, 89% coverage: 10:329/361 of query aligns to 18:343/378 of P69874
- C26 (≠ S18) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y19) mutation to L: Lower ATPase activity and transport efficiency.
- 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 (≠ I68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L127) mutation to M: Loss of ATPase activity and transport.
- D172 (= D164) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E287) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 88% coverage: 5:321/361 of query aligns to 2:313/353 of 1vciA
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 98% coverage: 9:361/361 of query aligns to 2:320/330 of 2awnA
3d31A Modbc from methanosarcina acetivorans (see paper)
41% identity, 76% coverage: 25:297/361 of query aligns to 16:284/348 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)
36% identity, 79% coverage: 10:293/361 of query aligns to 4:285/353 of 1oxvD
Query Sequence
>SM_b20630 FitnessBrowser__Smeli:SM_b20630
MANGISNKSVVLSDIRKSYGGLEVIHGIDLTIEEGDFVVFVGPSGCGKSTLLRMIAGLEE
VSEGEIAIKGRDVTDLDPSERGIAMVFQSYALYPHMSVSENLGFGLKMARTDPAEIARRV
AQVSAILKIDHLLDRRPGQLSGGQRQRVAIGRAIVRKPDVFLFDEPLSNLDAELRVSMRI
EIARLHRELGNTMVYVTHDQTEAMTLADQIVVLRDGRIEQAGSPRDVYEDPANMFVAGFI
GSPRMNFLDAEWQGDGTIRVGETTLEAAIDGGSLKHGERLLLGIRPEHIAVAEPGPERIA
AQVEFSEYLGGTRYLYCQLEDGQSLVVEQREGPNWQAGEKLSFAVPDDRRRFFAEDGRRL
R
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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