SitesBLAST
Comparing AO356_21610 FitnessBrowser__pseudo5_N2C3_1:AO356_21610 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)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
34% identity, 95% coverage: 1:347/364 of query aligns to 5:345/353 of 1vciA
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
31% identity, 95% coverage: 3:346/364 of query aligns to 7:366/375 of 2d62A
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)
33% identity, 90% coverage: 5:331/364 of query aligns to 6:335/393 of P9WQI3
- H193 (≠ T191) 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)
39% identity, 64% coverage: 3:235/364 of query aligns to 18:250/378 of P69874
- C26 (≠ T11) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ V12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S39) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ M61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L120) mutation to M: Loss of ATPase activity and transport.
- D172 (= D157) 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)
33% identity, 85% coverage: 2:312/364 of query aligns to 3:317/369 of P19566
- L86 (≠ N85) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P159) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D164) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E301) mutation to 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)
34% identity, 85% coverage: 2:312/364 of query aligns to 3:319/371 of P68187
- A85 (≠ I84) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S105) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ T116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R118) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E123) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G136) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D157) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ V227) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L240) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ P259) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G270) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ R273) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G275) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ V295) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E301) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
34% identity, 85% coverage: 2:312/364 of query aligns to 2:318/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ V12), S37 (≠ T37), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), Q81 (= Q81), R128 (= R128), A132 (≠ E132), S134 (= S134), G136 (= G136), Q137 (= Q137), E158 (= E158), H191 (≠ T191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
34% identity, 85% coverage: 2:312/364 of query aligns to 2:318/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ V12), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (= R128), S134 (= S134), Q137 (= Q137)
- binding beryllium trifluoride ion: S37 (≠ T37), G38 (≠ L38), K41 (= K41), Q81 (= Q81), S134 (= S134), G136 (= G136), H191 (≠ T191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
34% identity, 85% coverage: 2:312/364 of query aligns to 2:318/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ V12), V17 (≠ W17), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (= R128), A132 (≠ E132), S134 (= S134), Q137 (= Q137)
- binding tetrafluoroaluminate ion: S37 (≠ T37), G38 (≠ L38), K41 (= K41), Q81 (= Q81), S134 (= S134), G135 (= G135), G136 (= G136), E158 (= E158), H191 (≠ T191)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
34% identity, 85% coverage: 2:312/364 of query aligns to 2:318/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ V12), V17 (≠ W17), G38 (≠ L38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (= R128), A132 (≠ E132), S134 (= S134), Q137 (= Q137)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q81)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
34% identity, 85% coverage: 2:312/364 of query aligns to 2:318/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
35% identity, 80% coverage: 20:312/364 of query aligns to 18:316/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ T37), G36 (≠ L38), C37 (≠ S39), G38 (= G40), K39 (= K41), S40 (≠ T42), T41 (≠ S43), R126 (= R128), A130 (≠ E132), S132 (= S134), G134 (= G136), Q135 (= Q137)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
31% identity, 93% coverage: 15:352/364 of query aligns to 16:357/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (≠ T37), C40 (≠ S39), G41 (= G40), K42 (= K41), S43 (≠ T42), T44 (≠ S43), Q82 (= Q81), R129 (= R128), Q133 (≠ E132), S135 (= S134), G136 (= G135), G137 (= G136), Q159 (≠ E158), H192 (≠ T191)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q81)
Sites not aligning to the query:
1g291 Malk (see paper)
33% identity, 85% coverage: 2:312/364 of query aligns to 3:329/372 of 1g291
- binding magnesium ion: D69 (≠ H68), E71 (vs. gap), K72 (vs. gap), K79 (≠ R72), D80 (≠ L73), E292 (≠ S279), D293 (≠ H280)
- binding pyrophosphate 2-: S38 (≠ T37), G39 (≠ L38), C40 (≠ S39), G41 (= G40), K42 (= K41), T43 (= T42), T44 (≠ S43)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
31% identity, 93% coverage: 15:352/364 of query aligns to 16:358/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (≠ T37), G39 (≠ L38), G41 (= G40), K42 (= K41), S43 (≠ T42), Q82 (= Q81), Q133 (≠ E132), G136 (= G135), G137 (= G136), Q138 (= Q137), H192 (≠ T191)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q81)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
32% identity, 82% coverage: 15:314/364 of query aligns to 14:322/384 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)
36% identity, 73% coverage: 18:283/364 of query aligns to 21:283/353 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, 73% coverage: 18:283/364 of query aligns to 21:283/353 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, 73% coverage: 18:283/364 of query aligns to 21:283/353 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, 73% coverage: 18:283/364 of query aligns to 21:283/353 of Q97UY8
- S142 (= S134) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G136) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E158) 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
>AO356_21610 FitnessBrowser__pseudo5_N2C3_1:AO356_21610
MSLKLEHICRTVEGQTWIDDANLSFEPGSFNVLLGRTLSGKTSLMRLMAGLDKPDSGRIL
MNGVDVTHRPVRLRNVSMVYQQFINYPTMTVFENIASPLRQAGVSDEVIQSKVLETARML
RIEKFLQRHPLELSGGQQQRTAMARALVKDAELILFDEPLVNLDYKLREELRQEMRELFQ
ARHTIAVYATTEPNEALALGGTTTILHEGRVIQSGKSSSVYHQPQTVLAAELFSEPPINL
MPGRIAGNEVSFANFVHFPLNVDLRPVGEGEFRFGVRPSHISLVPSNDDDLELAVTVEVA
EISGSETFLHVRNEHFLLVLHLPGVHEYDVDAPIRIYIPTHKLFVFDAQGKLVQAPGQRI
ARVA
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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