SitesBLAST
Comparing AZOBR_RS26295 FitnessBrowser__azobra:AZOBR_RS26295 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 90% coverage: 1:319/354 of query aligns to 18:343/378 of P69874
- C26 (≠ A9) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y10) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F28) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S37) mutation to T: Loss of ATPase activity and transport.
- L60 (= L43) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I59) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V118) mutation to M: Loss of ATPase activity and transport.
- D172 (= D155) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ N259) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E275) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
46% identity, 75% coverage: 6:272/354 of query aligns to 9:298/372 of 1g291
- binding magnesium ion: D69 (= D66), E71 (vs. gap), K72 (vs. gap), K79 (≠ E70), D80 (≠ R71), E292 (≠ G266), D293 (≠ S267)
- binding pyrophosphate 2-: S38 (= S35), G39 (= G36), C40 (≠ S37), G41 (= G38), K42 (= K39), T43 (= T40), T44 (= T41)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
42% identity, 86% coverage: 1:304/354 of query aligns to 7:321/375 of 2d62A
8hprD Lpqy-sugabc in state 4 (see paper)
44% identity, 79% coverage: 1:278/354 of query aligns to 3:287/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y10), S38 (= S35), C40 (≠ S37), G41 (= G38), K42 (= K39), S43 (≠ T40), T44 (= T41), Q82 (= Q79), R129 (= R126), Q133 (≠ D130), S135 (= S132), G136 (= G133), G137 (= G134), Q159 (≠ E156), H192 (= H189)
- binding magnesium ion: S43 (≠ T40), Q82 (= Q79)
8hprC Lpqy-sugabc in state 4 (see paper)
44% identity, 79% coverage: 1:278/354 of query aligns to 3:287/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y10), S38 (= S35), G39 (= G36), G41 (= G38), K42 (= K39), S43 (≠ T40), Q82 (= Q79), Q133 (≠ D130), G136 (= G133), G137 (= G134), Q138 (= Q135), H192 (= H189)
- binding magnesium ion: S43 (≠ T40), Q82 (= Q79)
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 79% coverage: 1:278/354 of query aligns to 3:285/384 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)
45% identity, 79% coverage: 1:278/354 of query aligns to 4:288/393 of P9WQI3
- H193 (= H189) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 98% coverage: 1:348/354 of query aligns to 4:339/371 of P68187
- A85 (≠ S82) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P103) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V114) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E116) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G121) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G134) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D155) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R225) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L236) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W268) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ S290) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ Q294) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (vs. gap) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ T309) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ I315) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ E329) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
38% identity, 98% coverage: 1:348/354 of query aligns to 3:338/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y10), S37 (= S35), G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (= T41), Q81 (= Q79), R128 (= R126), A132 (≠ D130), S134 (= S132), G136 (= G134), Q137 (= Q135), E158 (= E156), H191 (= H189)
- binding magnesium ion: S42 (≠ T40), Q81 (= Q79)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 98% coverage: 1:348/354 of query aligns to 3:338/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y10), G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (= T41), R128 (= R126), S134 (= S132), Q137 (= Q135)
- binding beryllium trifluoride ion: S37 (= S35), G38 (= G36), K41 (= K39), Q81 (= Q79), S134 (= S132), G136 (= G134), H191 (= H189)
- binding magnesium ion: S42 (≠ T40), Q81 (= Q79)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 98% coverage: 1:348/354 of query aligns to 3:338/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y10), V17 (≠ A15), G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (= T41), R128 (= R126), A132 (≠ D130), S134 (= S132), Q137 (= Q135)
- binding tetrafluoroaluminate ion: S37 (= S35), G38 (= G36), K41 (= K39), Q81 (= Q79), S134 (= S132), G135 (= G133), G136 (= G134), E158 (= E156), H191 (= H189)
- binding magnesium ion: S42 (≠ T40), Q81 (= Q79)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 98% coverage: 1:348/354 of query aligns to 3:338/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y10), V17 (≠ A15), G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (= T41), R128 (= R126), A132 (≠ D130), S134 (= S132), Q137 (= Q135)
- binding magnesium ion: S42 (≠ T40), Q81 (= Q79)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 98% coverage: 1:348/354 of query aligns to 3:338/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 98% coverage: 1:348/354 of query aligns to 1:336/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y10), S35 (= S35), G36 (= G36), C37 (≠ S37), G38 (= G38), K39 (= K39), S40 (≠ T40), T41 (= T41), R126 (= R126), A130 (≠ D130), S132 (= S132), G134 (= G134), Q135 (= Q135)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 98% coverage: 1:348/354 of query aligns to 4:337/369 of P19566
- L86 (= L83) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P157) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D162) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ V297) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
47% identity, 68% coverage: 1:242/354 of query aligns to 7:242/353 of 1vciA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 70% coverage: 1:247/354 of query aligns to 4:257/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 70% coverage: 1:247/354 of query aligns to 4:257/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
42% identity, 70% coverage: 1:247/354 of query aligns to 4:257/353 of 1oxuA
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)
42% identity, 70% coverage: 1:247/354 of query aligns to 4:257/353 of Q97UY8
- S142 (= S132) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G134) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E156) 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
>AZOBR_RS26295 FitnessBrowser__azobra:AZOBR_RS26295
IEFQSVRKAYGSVKALHDFSLTIRPGEFLTILGSSGSGKTTALNALAGFSTADSGDIRID
GRSVIDEPPERRNLGMVFQNYSLFPHMSVFDNIAFPLRMRRMPRRDIKERVERVLEIVRL
GPLAGRMPRDLSGGQQQRVAFARAIVFEPPVLLMDEPLGALDLKLREALQFEIKEIQHQL
GCTVVYVTHDQREALAMSSRIVVLRDGRIEQVGTPSEMYDAPQSRFVADFIGQTNLLAAD
VAQPGSVAIPELGVTYRENAFTARPGSWYASIRPEKLQRRPAEGPDIAVSVTIQEAVFLG
DVIEYSARTDHGALIHFREQRRDRDRIPERGETANLVLRPSDVVLVPDLPRTGR
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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