SitesBLAST
Comparing Echvi_2123 FitnessBrowser__Cola:Echvi_2123 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1g291 Malk (see paper)
43% identity, 69% coverage: 19:238/318 of query aligns to 18:241/372 of 1g291
- binding magnesium ion: D69 (≠ N70), E71 (≠ A72), K72 (≠ Q73), K79 (≠ Y79), D80 (= D80)
- binding pyrophosphate 2-: S38 (= S39), G39 (= G40), C40 (≠ S41), G41 (= G42), K42 (= K43), T43 (≠ S44), T44 (≠ S45)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 75% coverage: 1:238/318 of query aligns to 4:244/375 of 2d62A
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 1:245/318 of query aligns to 1:249/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 1:245/318 of query aligns to 1:249/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
37% identity, 77% coverage: 1:245/318 of query aligns to 1:249/353 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)
37% identity, 77% coverage: 1:245/318 of query aligns to 1:249/353 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 (= E162) 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, 75% coverage: 4:243/318 of query aligns to 18:254/378 of P69874
- C26 (≠ R12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V32) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S41) mutation to T: Loss of ATPase activity and transport.
- L60 (= L47) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L63) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) 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.
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, 77% coverage: 1:245/318 of query aligns to 1:245/393 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.
8hprC Lpqy-sugabc in state 4 (see paper)
36% identity, 75% coverage: 9:245/318 of query aligns to 8:244/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S39), G39 (= G40), G41 (= G42), K42 (= K43), S43 (= S44), Q82 (= Q87), Q133 (= Q136), G136 (= G139), G137 (= G140), Q138 (= Q141), H192 (= H195)
- binding magnesium ion: S43 (= S44), Q82 (= Q87)
8hprD Lpqy-sugabc in state 4 (see paper)
36% identity, 75% coverage: 9:245/318 of query aligns to 8:244/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S39), C40 (≠ S41), G41 (= G42), K42 (= K43), S43 (= S44), T44 (≠ S45), Q82 (= Q87), R129 (≠ K132), Q133 (= Q136), S135 (= S138), G136 (= G139), G137 (= G140), Q159 (≠ E162), H192 (= H195)
- binding magnesium ion: S43 (= S44), Q82 (= Q87)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 99% coverage: 1:316/318 of query aligns to 1:289/369 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 (= 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
37% identity, 75% coverage: 1:238/318 of query aligns to 4:230/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 74% coverage: 9:244/318 of query aligns to 8:241/384 of 8hplC
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 99% coverage: 1:316/318 of query aligns to 1:291/371 of P68187
- A85 (≠ K90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ T117) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E122) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ R127) 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 (≠ L242) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W291) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G303) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ F307) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ D309) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 70% coverage: 21:244/318 of query aligns to 19:242/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
32% identity, 93% coverage: 21:316/318 of query aligns to 17:288/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S39), G36 (= G40), C37 (≠ S41), G38 (= G42), K39 (= K43), S40 (= S44), T41 (≠ S45), R126 (≠ K132), A130 (≠ Q136), S132 (= S138), G134 (= G140), Q135 (= Q141)
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
37% identity, 70% coverage: 21:244/318 of query aligns to 19:242/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S39), G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (≠ S45), Q81 (= Q87), R128 (≠ K132), A132 (≠ Q136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (= S44), Q81 (= Q87)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 70% coverage: 21:244/318 of query aligns to 19:242/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (≠ S45), R128 (≠ K132), S134 (= S138), Q137 (= Q141)
- binding beryllium trifluoride ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q87), S134 (= S138), G136 (= G140), H191 (= H195)
- binding magnesium ion: S42 (= S44), Q81 (= Q87)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 70% coverage: 21:244/318 of query aligns to 19:242/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (≠ S45), R128 (≠ K132), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding tetrafluoroaluminate ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q87), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (= S44), Q81 (= Q87)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 70% coverage: 21:244/318 of query aligns to 19:242/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G40), C39 (≠ S41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (≠ S45), R128 (≠ K132), A132 (≠ Q136), S134 (= S138), Q137 (= Q141)
- binding magnesium ion: S42 (= S44), Q81 (= Q87)
Sites not aligning to the query:
Query Sequence
>Echvi_2123 FitnessBrowser__Cola:Echvi_2123
MSYLKVSEVSKRYDAGSLALEDFSLQVKRGGVVSMVGESGSGKSSLLRIIAGLEVQSAGV
VHLGDQKILNPAQKLVPGYDEIQLIHQEYKLYPNSTVEENIARPLLLYDKAYQKERTAEI
LELLSLRAFKDKKPRQLSGGQQQKVAIGRALSIEPEVLLLDEPFSSLDAIQKRDLIEELK
EIFDALEVTVIFVTHDVDDALLMSEELLIIQKGKLLQQGNVREVFRKPASAYVARLFGYL
NLIPGAEEAYVRPSEVKITSKTSIKAEVVKQQFLIHYNLLTVKLEDSELFWKVDDPSRSV
NVGDEVFLDYQKEQLIQF
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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