SitesBLAST
Comparing SMc02519 FitnessBrowser__Smeli:SMc02519 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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, 97% coverage: 2:348/356 of query aligns to 7:347/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
33% identity, 98% coverage: 1:348/356 of query aligns to 4:369/375 of 2d62A
1g291 Malk (see paper)
35% identity, 88% coverage: 7:318/356 of query aligns to 9:336/372 of 1g291
- binding magnesium ion: D69 (≠ G67), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q71), D80 (≠ K72), E292 (≠ H278), D293 (≠ H279)
- binding pyrophosphate 2-: S38 (≠ T36), G39 (≠ L37), C40 (≠ S38), G41 (= G39), K42 (= K40), T43 (= T41), T44 (≠ S42)
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)
38% identity, 64% coverage: 1:229/356 of query aligns to 17:245/378 of P69874
- C26 (≠ V10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ V11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L29) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S38) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M44) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F60) 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.
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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
30% identity, 88% coverage: 2:316/356 of query aligns to 4:322/369 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
29% identity, 88% coverage: 2:316/356 of query aligns to 1:321/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ V11), S35 (≠ T36), G36 (≠ L37), C37 (≠ S38), G38 (= G39), K39 (= K40), S40 (≠ T41), T41 (≠ S42), R126 (= R127), A130 (≠ N131), S132 (= S133), G134 (= G135), Q135 (= Q136)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
29% identity, 88% coverage: 2:316/356 of query aligns to 4:324/371 of P68187
- A85 (≠ I83) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D104) 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 (= E117) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T122) 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 (≠ I226) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ T239) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ A258) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G269) 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 (≠ V294) 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 (≠ G314) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
29% identity, 88% coverage: 2:316/356 of query aligns to 3:323/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ V11), S37 (≠ T36), G38 (≠ L37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), Q81 (= Q80), R128 (= R127), A132 (≠ N131), S134 (= S133), G136 (= G135), Q137 (= Q136), E158 (= E157), H191 (≠ T190)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
29% identity, 88% coverage: 2:316/356 of query aligns to 3:323/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ V11), G38 (≠ L37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), R128 (= R127), S134 (= S133), Q137 (= Q136)
- binding beryllium trifluoride ion: S37 (≠ T36), G38 (≠ L37), K41 (= K40), Q81 (= Q80), S134 (= S133), G136 (= G135), H191 (≠ T190)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
29% identity, 88% coverage: 2:316/356 of query aligns to 3:323/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ V11), V17 (≠ H16), G38 (≠ L37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), R128 (= R127), A132 (≠ N131), S134 (= S133), Q137 (= Q136)
- binding tetrafluoroaluminate ion: S37 (≠ T36), G38 (≠ L37), K41 (= K40), Q81 (= Q80), S134 (= S133), G135 (= G134), G136 (= G135), E158 (= E157), H191 (≠ T190)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
29% identity, 88% coverage: 2:316/356 of query aligns to 3:323/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ V11), V17 (≠ H16), G38 (≠ L37), C39 (≠ S38), G40 (= G39), K41 (= K40), S42 (≠ T41), T43 (≠ S42), R128 (= R127), A132 (≠ N131), S134 (= S133), Q137 (= Q136)
- binding magnesium ion: S42 (≠ T41), Q81 (= Q80)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
29% identity, 88% coverage: 2:316/356 of query aligns to 3:323/374 of 2awnB
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)
30% identity, 91% coverage: 13:335/356 of query aligns to 16:340/393 of P9WQI3
- H193 (≠ T190) 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)
31% identity, 82% coverage: 22:312/356 of query aligns to 24:323/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (≠ T36), C40 (≠ S38), G41 (= G39), K42 (= K40), S43 (≠ T41), T44 (≠ S42), Q82 (= Q80), R129 (= R127), Q133 (≠ N131), S135 (= S133), G136 (= G134), G137 (= G135), Q159 (≠ E157), H192 (≠ T190)
- binding magnesium ion: S43 (≠ T41), Q82 (= Q80)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
31% identity, 83% coverage: 22:315/356 of query aligns to 22:324/384 of 8hplC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 63% coverage: 4:229/356 of query aligns to 6:238/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 63% coverage: 4:229/356 of query aligns to 6:238/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 63% coverage: 4:229/356 of query aligns to 6:238/353 of 1oxuA
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
35% identity, 63% coverage: 4:229/356 of query aligns to 6:238/353 of Q97UY8
- S142 (= S133) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G135) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E157) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
8hprC Lpqy-sugabc in state 4 (see paper)
31% identity, 81% coverage: 22:309/356 of query aligns to 24:320/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (≠ T36), G39 (≠ L37), G41 (= G39), K42 (= K40), S43 (≠ T41), Q82 (= Q80), Q133 (≠ N131), G136 (= G134), G137 (= G135), Q138 (= Q136), H192 (≠ T190)
- binding magnesium ion: S43 (≠ T41), Q82 (= Q80)
Sites not aligning to the query:
Query Sequence
>SMc02519 FitnessBrowser__Smeli:SMc02519
MLEMKKISKVVGGETHIHPTDLVLERGTLNVLLGPTLSGKTSLMRLMAGLDKPASGSIFF
DGADVTGVPVQKRSVAMVYQQFINYPAMTVYENIASPMRIKRADGATVDREVRKAAELLK
LTPYLDRTPLNLSGGQQQRTALARAIVKNADLVLLDEPLANLDYKLREELREELPKIFAA
SGAIFVYATTEPSEALLLGGNTATLSEGRITQFGRTIDVYRRPVDIVTARTFADPPLNTI
GLLKTGSQFVLEGKPVLAVPSHLRSLADGPCTVAFQPHHLSFGQPDGSDEPLTVKTAISE
ITGSESFIHVAFAGARWVMLAPGIHEIEPDAMLKVFVDTRHLMAFGPDGRAVGGMA
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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