SitesBLAST
Comparing Echvi_1022 FitnessBrowser__Cola:Echvi_1022 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
38% identity, 73% coverage: 1:252/345 of query aligns to 4:260/375 of 2d62A
1g291 Malk (see paper)
32% identity, 89% coverage: 1:308/345 of query aligns to 1:328/372 of 1g291
- binding magnesium ion: D69 (≠ N71), E71 (≠ K73), K72 (≠ S74), K79 (≠ N79), D80 (≠ Q80), E292 (= E278), D293 (= D279)
- binding pyrophosphate 2-: S38 (≠ N40), G39 (= G41), C40 (≠ S42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (= T46)
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 86% coverage: 1:295/345 of query aligns to 1:296/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 86% coverage: 1:295/345 of query aligns to 1:296/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 86% coverage: 1:295/345 of query aligns to 1:296/353 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)
35% identity, 86% coverage: 1:295/345 of query aligns to 1:296/353 of Q97UY8
- S142 (= S138) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G140) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (≠ D162) 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+).
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 82% coverage: 3:284/345 of query aligns to 17:303/378 of P69874
- C26 (≠ K12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ A124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E278) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
38% identity, 80% coverage: 4:278/345 of query aligns to 4:280/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (= F13), Q14 (≠ P14), T16 (= T16), V18 (≠ A20), S38 (≠ N40), G39 (= G41), C40 (≠ S42), G41 (= G43), K42 (= K44), T43 (= T45), T44 (= T46), R133 (≠ A132), E137 (≠ Q136), S139 (= S138), G141 (= G140), Q142 (= Q141)
- binding calcium ion: T43 (= T45), Q86 (= Q88)
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)
35% identity, 69% coverage: 1:238/345 of query aligns to 1:236/393 of P9WQI3
- H193 (= H195) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprD Lpqy-sugabc in state 4 (see paper)
34% identity, 74% coverage: 6:261/345 of query aligns to 5:263/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (≠ N40), C40 (≠ S42), G41 (= G43), K42 (= K44), S43 (≠ T45), T44 (= T46), Q82 (= Q88), R129 (≠ A132), Q133 (= Q136), S135 (= S138), G136 (≠ S139), G137 (= G140), Q159 (≠ D162), H192 (= H195)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q88)
8hprC Lpqy-sugabc in state 4 (see paper)
34% identity, 74% coverage: 6:261/345 of query aligns to 5:263/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (≠ N40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (≠ T45), Q82 (= Q88), Q133 (= Q136), G136 (≠ S139), G137 (= G140), Q138 (= Q141), H192 (= H195)
- binding magnesium ion: S43 (≠ T45), Q82 (= Q88)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
32% identity, 75% coverage: 1:258/345 of query aligns to 4:251/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
34% identity, 74% coverage: 6:261/345 of query aligns to 5:261/384 of 8hplC
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, 69% coverage: 1:238/345 of query aligns to 1:235/369 of P19566
- L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P163) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D168) 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)
35% identity, 79% coverage: 1:273/345 of query aligns to 1:256/371 of P68187
- A85 (= A91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I116) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D161) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ A231) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F258) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
35% identity, 78% coverage: 4:273/345 of query aligns to 3:255/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), S37 (≠ N40), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), Q81 (= Q88), R128 (≠ S129), A132 (≠ Q136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (≠ D162), H191 (= H195)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
35% identity, 78% coverage: 4:273/345 of query aligns to 3:255/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F13), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (≠ S129), S134 (= S138), Q137 (= Q141)
- binding beryllium trifluoride ion: S37 (≠ N40), G38 (= G41), K41 (= K44), Q81 (= Q88), S134 (= S138), G136 (= G140), H191 (= H195)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
35% identity, 78% coverage: 4:273/345 of query aligns to 3:255/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A20), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (≠ S129), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding tetrafluoroaluminate ion: S37 (≠ N40), G38 (= G41), K41 (= K44), Q81 (= Q88), S134 (= S138), G135 (≠ S139), G136 (= G140), E158 (≠ D162), H191 (= H195)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
35% identity, 78% coverage: 4:273/345 of query aligns to 3:255/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A20), G38 (= G41), C39 (≠ S42), G40 (= G43), K41 (= K44), S42 (≠ T45), T43 (= T46), R128 (≠ S129), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding magnesium ion: S42 (≠ T45), Q81 (= Q88)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 78% coverage: 4:273/345 of query aligns to 3:255/374 of 2awnB
Query Sequence
>Echvi_1022 FitnessBrowser__Cola:Echvi_1022
MSLLQLHGISKKFPQTKQFAVKDIHMEIEEGSVQAIVGENGSGKTTLLKLIAGLEHPDKG
EIVFSGQTIVNGKSALPANQREVGVIFQEYALFPQMTLLENVREALHQESRNARQIAMDS
LALAGLEDSFSAYPHQLSSGQRQRAALARALASRPKLLLLDDPFRSLDTRFKNEISEDIR
DIVKATGITAIVASHHAKDALSLADSIAILHKGILQQVGTPVEIYKKPANAYVANFFGKR
NELLATPTEDGFYAGFGFIPHPDSASYTDKVKILFRSEDAKIKKSTEQPLSGIVTRVLFY
GDHQIVKLEDDEGKQISIKAAPGRNFEMGARMFFTIDKFEIETAF
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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