SitesBLAST
Comparing WP_050997318.1 NCBI__GCF_000058485.1:WP_050997318.1 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
45% identity, 72% coverage: 1:294/410 of query aligns to 1:312/375 of 2d62A
1g291 Malk (see paper)
47% identity, 65% coverage: 12:278/410 of query aligns to 9:294/372 of 1g291
- binding magnesium ion: D69 (= D66), E71 (≠ T68), K72 (≠ S69), K79 (≠ H76), D80 (≠ R77), E292 (= E276), D293 (≠ H277)
- binding pyrophosphate 2-: S38 (= S41), G39 (= G42), C40 (≠ S43), G41 (= G44), K42 (= K45), T43 (≠ S46), T44 (= T47)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
43% identity, 69% coverage: 1:281/410 of query aligns to 1:281/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
46% identity, 66% coverage: 7:278/410 of query aligns to 3:286/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F16), S38 (= S41), G39 (= G42), G41 (= G44), K42 (= K45), S43 (= S46), Q82 (= Q85), Q133 (= Q137), G136 (= G140), G137 (= G141), Q138 (= Q142), H192 (= H196)
- binding magnesium ion: S43 (= S46), Q82 (= Q85)
8hprD Lpqy-sugabc in state 4 (see paper)
46% identity, 66% coverage: 7:278/410 of query aligns to 3:286/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F16), S38 (= S41), C40 (≠ S43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (= T47), Q82 (= Q85), R129 (= R133), Q133 (= Q137), S135 (= S139), G136 (= G140), G137 (= G141), Q159 (≠ E163), H192 (= H196)
- binding magnesium ion: S43 (= S46), Q82 (= Q85)
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 66% coverage: 7:278/410 of query aligns to 3:284/384 of 8hplC
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)
44% identity, 66% coverage: 7:278/410 of query aligns to 4:287/393 of P9WQI3
- H193 (= H196) 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)
36% identity, 97% coverage: 7:404/410 of query aligns to 4:357/369 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 (= P164) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D169) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E355) 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)
42% identity, 66% coverage: 7:278/410 of query aligns to 3:289/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 66% coverage: 7:278/410 of query aligns to 1:287/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F16), S35 (= S41), G36 (= G42), C37 (≠ S43), G38 (= G44), K39 (= K45), S40 (= S46), T41 (= T47), R126 (= R133), A130 (≠ Q137), S132 (= S139), G134 (= G141), Q135 (= Q142)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 66% coverage: 7:278/410 of query aligns to 4:290/371 of P68187
- A85 (= A88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ T121) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A128) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G141) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D162) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ V245) 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 (vs. gap) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ A270) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G272) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
42% identity, 66% coverage: 7:278/410 of query aligns to 3:289/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F16), S37 (= S41), G38 (= G42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), Q81 (= Q85), R128 (= R133), A132 (≠ Q137), S134 (= S139), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 66% coverage: 7:278/410 of query aligns to 3:289/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F16), G38 (= G42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (= R133), S134 (= S139), Q137 (= Q142)
- binding beryllium trifluoride ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q85), S134 (= S139), G136 (= G141), H191 (= H196)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 66% coverage: 7:278/410 of query aligns to 3:289/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F16), V17 (≠ A21), G38 (= G42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (= R133), A132 (≠ Q137), S134 (= S139), Q137 (= Q142)
- binding tetrafluoroaluminate ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q85), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 66% coverage: 7:278/410 of query aligns to 3:289/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F16), V17 (≠ A21), G38 (= G42), C39 (≠ S43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (= R133), A132 (≠ Q137), S134 (= S139), Q137 (= Q142)
- binding magnesium ion: S42 (= S46), Q81 (= Q85)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 57% coverage: 12:243/410 of query aligns to 23:253/378 of P69874
- C26 (≠ S15) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F16) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I34) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S43) mutation to T: Loss of ATPase activity and transport.
- L60 (= L49) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F65) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L125) mutation to M: Loss of ATPase activity and transport.
- D172 (= D162) 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 62% coverage: 24:278/410 of query aligns to 13:259/344 of 2awnC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 67% coverage: 17:289/410 of query aligns to 16:292/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 67% coverage: 17:289/410 of query aligns to 16:292/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
39% identity, 67% coverage: 17:289/410 of query aligns to 16:292/353 of 1oxuA
Sites not aligning to the query:
Query Sequence
>WP_050997318.1 NCBI__GCF_000058485.1:WP_050997318.1
MVTGVPIEFDRIGRSFGSVHALHEVSLTVAAGEIVALLGPSGSGKSTLLRICAGLDEPTT
GDVRFDGTSQLGLPPHRRDVSMVFQHFALYPHKSALDNLTLALRHGRGLPKAAAVARARE
TLAMLGIAELAGRRPPQMSGGQRQRVAIGRALATRARVILLDEPMSGLDAQLRVELRVEI
VGLLRSLGTTALFVTHDQAEAMAVGDRVAVLGEGRLQQIGTPDEIYDRPATRFVAAFVGS
PPMNVWDGHWHDGRLRADGFDVPAPAGAAAFGVRPEHLTLDLGALDVDSPGAGTPGVGTP
GVGTPGVGTPGVGTPGVGGLDGGSLDVGVPEQPGSLRGVGGSEQLRLSGEVVVSERLGAE
RTVHVRTRAGVLAVRVNAALALTPGAFVVLRAPTSALTYFAPDGDRLDHP
Or try a new SitesBLAST search
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