SitesBLAST
Comparing BPHYT_RS30485 FitnessBrowser__BFirm:BPHYT_RS30485 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
46% identity, 71% coverage: 9:263/360 of query aligns to 7:269/375 of 2d62A
1g291 Malk (see paper)
46% identity, 71% coverage: 8:263/360 of query aligns to 3:266/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ H78), D80 (≠ K79)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (≠ S45), G41 (= G46), K42 (= K47), T43 (= T48), T44 (= T49)
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)
42% identity, 86% coverage: 27:334/360 of query aligns to 36:348/378 of P69874
- F45 (= F36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ T260) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E281) 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 89% coverage: 9:330/360 of query aligns to 4:321/371 of P68187
- A85 (= A90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ A233) 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 (≠ L275) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ D286) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ G290) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G292) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G310) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A317) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 89% coverage: 9:330/360 of query aligns to 1:318/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y18), S35 (= S43), G36 (= G44), C37 (≠ S45), G38 (= G46), K39 (= K47), S40 (≠ T48), T41 (= T49), R126 (= R134), A130 (≠ Q138), S132 (= S140), G134 (= G142), Q135 (= Q143)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
39% identity, 89% coverage: 9:330/360 of query aligns to 3:320/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y18), S37 (= S43), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), Q81 (= Q87), R128 (= R134), A132 (≠ Q138), S134 (= S140), G136 (= G142), Q137 (= Q143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 89% coverage: 9:330/360 of query aligns to 3:320/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R134), S134 (= S140), Q137 (= Q143)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 89% coverage: 9:330/360 of query aligns to 3:320/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), V17 (≠ A23), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R134), A132 (≠ Q138), S134 (= S140), Q137 (= Q143)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q87), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 89% coverage: 9:330/360 of query aligns to 3:320/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y18), V17 (≠ A23), G38 (= G44), C39 (≠ S45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (= R134), A132 (≠ Q138), S134 (= S140), Q137 (= Q143)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q87)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 89% coverage: 9:330/360 of query aligns to 3:320/374 of 2awnB
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 68% coverage: 9:252/360 of query aligns to 7:243/353 of 1vciA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
39% identity, 90% coverage: 9:331/360 of query aligns to 4:320/369 of P19566
- L86 (= L91) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ A317) 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)
51% identity, 61% coverage: 23:240/360 of query aligns to 19:236/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
49% identity, 61% coverage: 23:240/360 of query aligns to 16:233/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
49% identity, 63% coverage: 16:240/360 of query aligns to 10:235/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y18), S38 (= S43), C40 (≠ S45), G41 (= G46), K42 (= K47), S43 (≠ T48), T44 (= T49), Q82 (= Q87), R129 (= R134), Q133 (= Q138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q87)
8hprC Lpqy-sugabc in state 4 (see paper)
49% identity, 63% coverage: 16:240/360 of query aligns to 10:235/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y18), S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (≠ T48), Q82 (= Q87), Q133 (= Q138), G136 (= G141), G137 (= G142), Q138 (= Q143), H192 (= H197)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q87)
3d31A Modbc from methanosarcina acetivorans (see paper)
36% identity, 85% coverage: 9:315/360 of query aligns to 2:307/348 of 3d31A
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 88% coverage: 14:330/360 of query aligns to 1:290/344 of 2awnC
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
41% identity, 66% coverage: 13:251/360 of query aligns to 10:255/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
41% identity, 66% coverage: 13:251/360 of query aligns to 10:255/353 of 1oxvA
Query Sequence
>BPHYT_RS30485 FitnessBrowser__BFirm:BPHYT_RS30485
MDARAKTGVSIRSAAKRYGQVVALDDVSLDIAPGEFVSLLGPSGSGKTTLLGILGGFVQP
SSGAVWVGERDITFAPPHKRDIGIVFQNYALFPHMSVGENVAFPLRARRQPKGTWAKKVA
DALAMVELSGYESRGISQLSGGQRQRVALARAMVFEPQLILMDEPLSALDKQLRETMQIE
LRRLHRKLGATIVYVTHDQREALTMSDRVAVLKNGRLVQIDTPERLYDRPCDAFVASFIG
EATLLDVTRAGDDAVRLGDTVLRTAHPLPHGNKLLLAVQTEKLVIDGGGGGGNDGVNRLS
CRVTEVLYQGESLRVFAALADGTAISLRQPGGHDARRRIPEPGAQMSVTLDPQDTIVVPA
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