SitesBLAST
Comparing GFF3011 FitnessBrowser__Marino:GFF3011 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)
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, 100% coverage: 1:372/372 of query aligns to 1:391/393 of P9WQI3
- H193 (= H194) 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, 98% coverage: 2:365/372 of query aligns to 1:356/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (= S45), Q82 (= Q84), Q133 (≠ N135), G136 (= G138), G137 (= G139), Q138 (= Q140), H192 (= H194)
- binding magnesium ion: S43 (= S45), Q82 (= Q84)
8hprD Lpqy-sugabc in state 4 (see paper)
48% identity, 98% coverage: 2:365/372 of query aligns to 1:355/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S40), C40 (= C42), G41 (= G43), K42 (= K44), S43 (= S45), T44 (= T46), Q82 (= Q84), R129 (≠ K131), Q133 (≠ N135), S135 (= S137), G136 (= G138), G137 (= G139), Q159 (≠ E161), H192 (= H194)
- binding magnesium ion: S43 (= S45), Q82 (= Q84)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
46% identity, 99% coverage: 1:369/372 of query aligns to 4:374/375 of 2d62A
8hplC Lpqy-sugabc in state 1 (see paper)
46% identity, 98% coverage: 2:365/372 of query aligns to 1:377/384 of 8hplC
1g291 Malk (see paper)
46% identity, 99% coverage: 1:369/372 of query aligns to 1:371/372 of 1g291
- binding magnesium ion: D69 (≠ T71), E71 (= E73), K72 (vs. gap), K79 (= K75), D80 (= D76), E292 (= E290), D293 (≠ H291), K359 (= K357)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (≠ S45), T44 (= T46)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
45% identity, 99% coverage: 1:370/372 of query aligns to 4:353/353 of 1vciA
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
48% identity, 91% coverage: 1:337/372 of query aligns to 1:320/371 of P68187
- A85 (= A87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V119) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D121) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S126) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G139) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D160) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F243) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ K268) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G280) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ I284) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G286) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G308) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E316) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
48% identity, 91% coverage: 1:337/372 of query aligns to 1:318/369 of P19566
- L86 (= L88) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P162) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D167) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E316) 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)
48% identity, 90% coverage: 2:337/372 of query aligns to 1:319/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
48% identity, 90% coverage: 2:337/372 of query aligns to 1:319/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S40), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), Q81 (= Q84), R128 (≠ K131), A132 (≠ N135), S134 (= S137), G136 (= G139), Q137 (= Q140), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (= S45), Q81 (= Q84)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
48% identity, 90% coverage: 2:337/372 of query aligns to 1:319/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (≠ K131), S134 (= S137), Q137 (= Q140)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q84), S134 (= S137), G136 (= G139), H191 (= H194)
- binding magnesium ion: S42 (= S45), Q81 (= Q84)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
48% identity, 90% coverage: 2:337/372 of query aligns to 1:319/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ T20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (≠ K131), A132 (≠ N135), S134 (= S137), Q137 (= Q140)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q84), S134 (= S137), G135 (= G138), G136 (= G139), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (= S45), Q81 (= Q84)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
48% identity, 90% coverage: 2:337/372 of query aligns to 1:319/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (≠ T20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (≠ K131), A132 (≠ N135), S134 (= S137), Q137 (= Q140)
- binding magnesium ion: S42 (= S45), Q81 (= Q84)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
48% identity, 90% coverage: 4:337/372 of query aligns to 1:317/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S40), G36 (= G41), C37 (= C42), G38 (= G43), K39 (= K44), S40 (= S45), T41 (= T46), R126 (≠ K131), A130 (≠ N135), S132 (= S137), G134 (= G139), Q135 (= Q140)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
47% identity, 85% coverage: 22:337/372 of query aligns to 12:289/344 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)
40% identity, 94% coverage: 4:353/372 of query aligns to 18:372/378 of P69874
- C26 (≠ T12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C42) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L123) mutation to M: Loss of ATPase activity and transport.
- D172 (= D160) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ V267) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E290) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 90% coverage: 2:337/372 of query aligns to 1:277/330 of 2awnA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 97% coverage: 1:362/372 of query aligns to 1:351/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
34% identity, 97% coverage: 1:362/372 of query aligns to 1:351/353 of 1oxvA
Query Sequence
>GFF3011 FitnessBrowser__Marino:GFF3011
MSQLELRSIRKTYPGVAEETLKGIDIDIASGEFLILVGPSGCGKSTLMNTIAGLETITDG
SIVLDGKDISTMEPKDRDIAMVFQSYALYPTMSVRENIAFGLKIRGLPKHEIDQEVERVA
DLLQISPLMNKKPANLSGGQQQRVAMGRALARRPRIYLFDEPLSNLDAKLRVEMRTEIKK
LHQRLKTTIVYVTHDQIEAMTLADRIAVLKDGELQQLGTPKEVYDRPENLFVAGFMGSPA
MSFVPVTVEQGEGGLQAEVRGNDGRSVKLPVPEFLADRVGKKVILGIRPEHITQPQDQKN
DQTLVAKGEFTIEVTEPTGPDVIALIQLNDTNVHCRIDPEHPVTWGETAELMFDMKKVVF
FDPETEKRIAPH
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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