SitesBLAST
Comparing 3609745 FitnessBrowser__Dino:3609745 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)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
34% identity, 99% coverage: 2:351/353 of query aligns to 7:350/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
33% identity, 99% coverage: 2:351/353 of query aligns to 7:372/375 of 2d62A
8hplC Lpqy-sugabc in state 1 (see paper)
35% identity, 88% coverage: 2:310/353 of query aligns to 3:319/384 of 8hplC
8hprC Lpqy-sugabc in state 4 (see paper)
33% identity, 97% coverage: 2:345/353 of query aligns to 3:352/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ V11), S38 (≠ T36), G39 (= G37), G41 (= G39), K42 (= K40), S43 (≠ T41), Q82 (= Q80), Q133 (≠ E131), G136 (= G134), G137 (= G135), Q138 (= Q136), H192 (≠ S190)
- binding magnesium ion: S43 (≠ T41), Q82 (= Q80)
8hprD Lpqy-sugabc in state 4 (see paper)
35% identity, 88% coverage: 2:310/353 of query aligns to 3:321/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ V11), S38 (≠ T36), C40 (≠ T38), G41 (= G39), K42 (= K40), S43 (≠ T41), T44 (≠ S42), Q82 (= Q80), R129 (= R127), Q133 (≠ E131), S135 (= S133), G136 (= G134), G137 (= G135), Q159 (≠ E157), H192 (≠ S190)
- binding magnesium ion: S43 (≠ T41), Q82 (= Q80)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 1:356/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ V11), S35 (≠ T36), G36 (= G37), C37 (≠ T38), G38 (= G39), K39 (= K40), S40 (≠ T41), T41 (≠ S42), R126 (= R127), A130 (≠ E131), S132 (= S133), G134 (= G135), Q135 (= Q136)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 4:357/369 of P19566
- L86 (≠ N84) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P158) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D163) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E300) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 3:358/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 99% coverage: 2:349/353 of query aligns to 4:359/371 of P68187
- A85 (≠ V83) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A104) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A115) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D117) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ R122) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G135) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D156) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L226) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (vs. gap) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W257) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ D268) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ T272) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ A274) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G294) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E300) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ D314) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G330) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ Y336) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F345) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1g291 Malk (see paper)
36% identity, 90% coverage: 2:318/353 of query aligns to 4:336/372 of 1g291
- binding magnesium ion: D69 (≠ K67), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q71), D80 (≠ K72), E292 (≠ H278), D293 (≠ R279)
- binding pyrophosphate 2-: S38 (≠ T36), G39 (= G37), C40 (≠ T38), G41 (= G39), K42 (= K40), T43 (= T41), T44 (≠ S42)
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 3:358/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ V11), S37 (≠ T36), G38 (= G37), C39 (≠ T38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), Q81 (= Q80), R128 (= R127), A132 (≠ E131), S134 (= S133), G136 (= G135), Q137 (= Q136), E158 (= E157), H191 (≠ S190)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 3:358/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ V11), G38 (= G37), C39 (≠ T38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), R128 (= R127), S134 (= S133), Q137 (= Q136)
- binding beryllium trifluoride ion: S37 (≠ T36), G38 (= G37), K41 (= K40), Q81 (= Q80), S134 (= S133), G136 (= G135), H191 (≠ S190)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 3:358/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ V11), V17 (≠ H16), G38 (= G37), C39 (≠ T38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), R128 (= R127), A132 (≠ E131), S134 (= S133), Q137 (= Q136)
- binding tetrafluoroaluminate ion: S37 (≠ T36), G38 (= G37), K41 (= K40), Q81 (= Q80), S134 (= S133), G135 (= G134), G136 (= G135), E158 (= E157), H191 (≠ S190)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
32% identity, 99% coverage: 2:349/353 of query aligns to 3:358/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ V11), V17 (≠ H16), G38 (= G37), C39 (≠ T38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), R128 (= R127), A132 (≠ E131), S134 (= S133), Q137 (= Q136)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 77% coverage: 17:287/353 of query aligns to 33:306/378 of P69874
- F45 (= F29) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ T38) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I44) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ M60) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L119) mutation to M: Loss of ATPase activity and transport.
- D172 (= D156) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (≠ H278) 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.
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)
36% identity, 83% coverage: 15:306/353 of query aligns to 18:313/393 of P9WQI3
- H193 (≠ S190) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
31% identity, 95% coverage: 14:349/353 of query aligns to 8:328/344 of 2awnC
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
28% identity, 97% coverage: 2:345/353 of query aligns to 4:350/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
28% identity, 97% coverage: 2:345/353 of query aligns to 4:350/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
28% identity, 97% coverage: 2:345/353 of query aligns to 4:350/353 of 1oxuA
Query Sequence
>3609745 FitnessBrowser__Dino:3609745
MIELQEVTKRVGRVTHIKPTSLVFHPGEFNVLLGATGTGKTSLIKLMAGLDPMASGRILM
GGQDVTKLNTQKRQISLVHQFFVNYPHMSVFENIASPLRVAGMAKSEIQGRVEEAADLLQ
LRPMLHRKPNELSGGQQQRTALARAIAKDSRAVFLDEPLANLDYKLREELREQLPELFAG
RGAVVVYATSEPEEALMLGGRTALMDDGRVTQFGPTAQVYREPENLTAARVFSDPPINAA
EITKQGAQIRMQNGAGWEVSGPPAALPDGRYTVAVRPHRVTPQRSHDAEVELRGTVLVTE
LSGSESSAHFRLGDTDWVSLAHGVHPYKVGEEHVFYMNPENCRYFGTDGKRVA
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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