SitesBLAST
Comparing Ga0059261_3668 FitnessBrowser__Korea:Ga0059261_3668 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)
3d31A Modbc from methanosarcina acetivorans (see paper)
40% identity, 92% coverage: 15:198/201 of query aligns to 18:198/348 of 3d31A
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 92% coverage: 16:199/201 of query aligns to 22:205/369 of P19566
- L86 (= L87) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P154) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D159) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 92% coverage: 16:199/201 of query aligns to 22:205/371 of P68187
- A85 (≠ R86) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D104) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L111) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A113) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A118) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G131) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D152) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 267 W→G: Normal maltose transport but constitutive mal gene expression.
- 278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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, 92% coverage: 16:199/201 of query aligns to 21:204/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S33), G38 (= G34), C39 (≠ V35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (≠ S39), Q81 (= Q83), R128 (= R123), A132 (≠ S127), S134 (= S129), G136 (= G131), Q137 (≠ E132), E158 (= E153), H191 (= H186)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q83)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 92% coverage: 16:199/201 of query aligns to 21:204/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G34), C39 (≠ V35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (≠ S39), R128 (= R123), S134 (= S129), Q137 (≠ E132)
- binding beryllium trifluoride ion: S37 (= S33), G38 (= G34), K41 (= K37), Q81 (= Q83), S134 (= S129), G136 (= G131), H191 (= H186)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q83)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 92% coverage: 16:199/201 of query aligns to 21:204/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G34), C39 (≠ V35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (≠ S39), R128 (= R123), A132 (≠ S127), S134 (= S129), Q137 (≠ E132)
- binding tetrafluoroaluminate ion: S37 (= S33), G38 (= G34), K41 (= K37), Q81 (= Q83), S134 (= S129), G135 (= G130), G136 (= G131), E158 (= E153), H191 (= H186)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q83)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 92% coverage: 16:199/201 of query aligns to 21:204/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G34), C39 (≠ V35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (≠ S39), R128 (= R123), A132 (≠ S127), S134 (= S129), Q137 (≠ E132)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q83)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 97% coverage: 5:198/201 of query aligns to 10:213/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 92% coverage: 16:199/201 of query aligns to 21:204/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 92% coverage: 16:199/201 of query aligns to 19:202/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S33), G36 (= G34), C37 (≠ V35), G38 (= G36), K39 (= K37), S40 (≠ T38), T41 (≠ S39), R126 (= R123), A130 (≠ S127), S132 (= S129), G134 (= G131), Q135 (≠ E132)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
39% identity, 92% coverage: 15:199/201 of query aligns to 19:203/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 92% coverage: 15:199/201 of query aligns to 21:205/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S33), G39 (= G34), G41 (= G36), K42 (= K37), S43 (≠ T38), Q82 (= Q83), Q133 (≠ S127), G136 (= G130), G137 (= G131), Q138 (≠ E132), H192 (= H186)
- binding magnesium ion: S43 (≠ T38), Q82 (= Q83)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 92% coverage: 15:199/201 of query aligns to 21:205/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S33), C40 (≠ V35), G41 (= G36), K42 (= K37), S43 (≠ T38), T44 (≠ S39), Q82 (= Q83), R129 (= R123), Q133 (≠ S127), S135 (= S129), G136 (= G130), G137 (= G131), Q159 (≠ E153), H192 (= H186)
- binding magnesium ion: S43 (≠ T38), Q82 (= Q83)
Sites not aligning to the query:
1g291 Malk (see paper)
38% identity, 92% coverage: 15:198/201 of query aligns to 21:210/372 of 1g291
- binding magnesium ion: D69 (= D64), E71 (≠ A66), K72 (≠ I67), K79 (≠ E74), D80 (≠ R75)
- binding pyrophosphate 2-: S38 (= S33), G39 (= G34), C40 (≠ V35), G41 (= G36), K42 (= K37), T43 (= T38), T44 (≠ S39)
Sites not aligning to the query:
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)
37% identity, 92% coverage: 16:199/201 of query aligns to 23:206/393 of P9WQI3
- H193 (= H186) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
36% identity, 92% coverage: 15:199/201 of query aligns to 35:219/378 of P69874
- F45 (≠ I26) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ V35) mutation to T: Loss of ATPase activity and transport.
- L60 (= L41) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V57) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (vs. gap) mutation to M: Loss of ATPase activity and transport.
- D172 (= D152) mutation to N: 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.
- 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 92% coverage: 15:198/201 of query aligns to 23:211/353 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)
36% identity, 92% coverage: 15:198/201 of query aligns to 23:211/353 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)
36% identity, 92% coverage: 15:198/201 of query aligns to 23:211/353 of 1oxuA
Sites not aligning to the query:
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)
36% identity, 92% coverage: 15:198/201 of query aligns to 23:211/353 of Q97UY8
- S142 (= S129) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G131) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E153) 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+).
Query Sequence
>Ga0059261_3668 FitnessBrowser__Korea:Ga0059261_3668
MSFDIAIEKRRGDAQISCRIEGGEGIIVLFGPSGVGKTSVLDMVAGLLEPDTGHVRVGGE
TLFDAAIGEDVPPERRRAGYVFQDARLFPHLSVRANLLYGAGGDPSGLGDLAARFDIAHL
LDRWPRSLSGGEARRVAIGRALLAKPRFLLLDEPLSSLDRARREEVTRVIERLRDEAALP
ILMVTHDPVEAERLGQRIIEI
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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