SitesBLAST
Comparing Dsui_1109 FitnessBrowser__PS:Dsui_1109 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)
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
33% identity, 94% coverage: 15:263/266 of query aligns to 4:253/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
33% identity, 94% coverage: 15:263/266 of query aligns to 4:253/253 of 1g9xB
6mjpA Lptb(e163q)fgc from vibrio cholerae (see paper)
33% identity, 94% coverage: 15:263/266 of query aligns to 2:235/240 of 6mjpA
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
32% identity, 88% coverage: 16:248/266 of query aligns to 1:215/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F25), S35 (≠ N50), G36 (= G51), C37 (≠ A52), G38 (= G53), K39 (= K54), S40 (= S55), T41 (≠ S56), R126 (≠ T159), A130 (≠ R163), S132 (≠ P165), G134 (= G167), Q135 (≠ L168)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
32% identity, 88% coverage: 16:248/266 of query aligns to 3:217/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F25), S37 (≠ N50), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (≠ S56), Q81 (= Q97), R128 (≠ T159), A132 (≠ R163), S134 (≠ P165), G136 (= G167), Q137 (≠ L168), E158 (= E189), H191 (= H222)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
32% identity, 88% coverage: 16:248/266 of query aligns to 3:217/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F25), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (≠ S56), R128 (≠ T159), S134 (≠ P165), Q137 (≠ L168)
- binding beryllium trifluoride ion: S37 (≠ N50), G38 (= G51), K41 (= K54), Q81 (= Q97), S134 (≠ P165), G136 (= G167), H191 (= H222)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
32% identity, 88% coverage: 16:248/266 of query aligns to 3:217/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (≠ S56), R128 (≠ T159), A132 (≠ R163), S134 (≠ P165), Q137 (≠ L168)
- binding tetrafluoroaluminate ion: S37 (≠ N50), G38 (= G51), K41 (= K54), Q81 (= Q97), S134 (≠ P165), G135 (≠ Y166), G136 (= G167), E158 (= E189), H191 (= H222)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
32% identity, 88% coverage: 16:248/266 of query aligns to 3:217/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F25), V17 (≠ A30), G38 (= G51), C39 (≠ A52), G40 (= G53), K41 (= K54), S42 (= S55), T43 (≠ S56), R128 (≠ T159), A132 (≠ R163), S134 (≠ P165), Q137 (≠ L168)
- binding magnesium ion: S42 (= S55), Q81 (= Q97)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 88% coverage: 16:248/266 of query aligns to 4:218/371 of P68187
- A85 (= A100) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ Q134) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V144) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V147) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D149) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q154) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G167) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D188) 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 89% coverage: 18:254/266 of query aligns to 6:231/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 89% coverage: 18:254/266 of query aligns to 6:231/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 89% coverage: 18:254/266 of query aligns to 6:231/353 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)
31% identity, 89% coverage: 18:254/266 of query aligns to 6:231/353 of Q97UY8
- S142 (≠ P165) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G167) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E189) 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+).
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
32% identity, 88% coverage: 16:248/266 of query aligns to 3:217/374 of 2awnB
6mhzA Vanadate trapped cryo-em structure of e.Coli lptb2fg transporter (see paper)
29% identity, 93% coverage: 16:263/266 of query aligns to 3:235/235 of 6mhzA
- binding adp orthovanadate: Y12 (≠ F25), N37 (= N50), G38 (= G51), G40 (= G53), K41 (= K54), T42 (≠ S55), T43 (≠ S56), Q84 (= Q97), S136 (≠ R163), S138 (≠ P165), G139 (≠ Y166), G140 (= G167), E162 (= E189), G166 (= G193), H194 (= H222)
6s8nB Cryo-em structure of lptb2fgc in complex with lipopolysaccharide (see paper)
29% identity, 93% coverage: 16:263/266 of query aligns to 3:235/238 of 6s8nB
6s8gA Cryo-em structure of lptb2fgc in complex with amp-pnp (see paper)
29% identity, 93% coverage: 16:263/266 of query aligns to 3:235/238 of 6s8gA
- binding phosphoaminophosphonic acid-adenylate ester: Y12 (≠ F25), R15 (≠ V28), N37 (= N50), G40 (= G53), K41 (= K54), T42 (≠ S55), T43 (≠ S56), Q84 (= Q97), S136 (≠ R163), S138 (≠ P165), E141 (≠ L168)
1ji0A Crystal structure analysis of the abc transporter from thermotoga maritima
28% identity, 96% coverage: 11:265/266 of query aligns to 2:240/240 of 1ji0A
6mbnA Lptb e163q in complex with atp (see paper)
29% identity, 93% coverage: 16:263/266 of query aligns to 4:236/241 of 6mbnA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
31% identity, 88% coverage: 16:248/266 of query aligns to 4:218/369 of P19566
- L86 (= L101) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P190) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ N195) 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.
Query Sequence
>Dsui_1109 FitnessBrowser__PS:Dsui_1109
MSEQNQNGRRVGEVILDLQNISLRFGGVKALTDISFNVKEHEIRAIIGPNGAGKSSMLNV
INGVYHPQEGRIVFHGEERKKMEPHMAATQGIARTFQNIALFKGMSVLDNIMTGRITKMK
CGFLEQALYLGRAQKEELAHREKVEEVIDFLEIQHIRKTPVGRLPYGLQKRVELGRALAA
EPSLLLLDEPMAGMNVEEKQDMCRFILDVNDQFGTTIVLIEHDMGVVMDISDRMVVLDYG
KKIGDGTPDDVRNNQEVISAYLGVAH
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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