SitesBLAST
Comparing 3609156 FitnessBrowser__Dino:3609156 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)
36% identity, 81% coverage: 16:232/269 of query aligns to 15:228/378 of P69874
- C26 (≠ T27) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y28) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F48) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C57) mutation to T: Loss of ATPase activity and transport.
- L60 (= L63) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L79) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V137) mutation to M: Loss of ATPase activity and transport.
- D172 (= D174) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
35% identity, 78% coverage: 14:223/269 of query aligns to 2:216/375 of 2d62A
1g291 Malk (see paper)
36% identity, 76% coverage: 21:224/269 of query aligns to 6:214/372 of 1g291
- binding magnesium ion: D69 (≠ E82), E71 (≠ V84), K72 (≠ R85), K79 (≠ A87), D80 (≠ R88)
- binding pyrophosphate 2-: S38 (= S55), G39 (= G56), C40 (= C57), G41 (= G58), K42 (= K59), T43 (≠ S60), T44 (= T61)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 80% coverage: 20:233/269 of query aligns to 4:214/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 80% coverage: 20:233/269 of query aligns to 4:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y28), S37 (= S55), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), Q81 (= Q96), R128 (≠ V145), A132 (≠ E149), S134 (= S151), G136 (= G153), Q137 (≠ M154), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 80% coverage: 20:233/269 of query aligns to 4:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y28), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (≠ V145), S134 (= S151), Q137 (≠ M154)
- binding beryllium trifluoride ion: S37 (= S55), G38 (= G56), K41 (= K59), Q81 (= Q96), S134 (= S151), G136 (= G153), H191 (= H208)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 80% coverage: 20:233/269 of query aligns to 4:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y28), V17 (≠ A35), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (≠ V145), A132 (≠ E149), S134 (= S151), Q137 (≠ M154)
- binding tetrafluoroaluminate ion: S37 (= S55), G38 (= G56), K41 (= K59), Q81 (= Q96), S134 (= S151), G135 (= G152), G136 (= G153), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 80% coverage: 20:233/269 of query aligns to 4:214/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y28), V17 (≠ A35), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (≠ V145), A132 (≠ E149), S134 (= S151), Q137 (≠ M154)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
35% identity, 80% coverage: 20:233/269 of query aligns to 5:215/371 of P68187
- A85 (≠ T99) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ M127) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A130) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E132) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V137) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G153) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D174) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
35% identity, 80% coverage: 20:233/269 of query aligns to 2:212/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y28), S35 (= S55), G36 (= G56), C37 (= C57), G38 (= G58), K39 (= K59), S40 (= S60), T41 (= T61), R126 (≠ V145), A130 (≠ E149), S132 (= S151), G134 (= G153), Q135 (≠ M154)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
36% identity, 80% coverage: 20:233/269 of query aligns to 5:215/369 of P19566
- L86 (= L100) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P176) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D181) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
33% identity, 79% coverage: 21:233/269 of query aligns to 20:244/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
33% identity, 79% coverage: 21:233/269 of query aligns to 20:244/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
7ahdC Opua (e190q) occluded (see paper)
33% identity, 79% coverage: 21:233/269 of query aligns to 20:244/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (vs. gap), S61 (= S55), G62 (= G56), G64 (= G58), K65 (= K59), S66 (= S60), T67 (= T61), Q111 (= Q96), K161 (≠ N148), Q162 (≠ E149), S164 (= S151), G166 (= G153), M167 (= M154), Q188 (≠ E175), H221 (= H208)
Sites not aligning to the query:
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)
36% identity, 75% coverage: 21:223/269 of query aligns to 6:208/393 of P9WQI3
- H193 (= H208) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
37% identity, 72% coverage: 20:213/269 of query aligns to 3:209/232 of 1f3oA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
33% identity, 75% coverage: 21:223/269 of query aligns to 6:214/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
33% identity, 75% coverage: 21:223/269 of query aligns to 6:214/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
33% identity, 75% coverage: 21:223/269 of query aligns to 6:214/353 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)
33% identity, 75% coverage: 21:223/269 of query aligns to 6:214/353 of Q97UY8
- S142 (= S151) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G153) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E175) 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
>3609156 FitnessBrowser__Dino:3609156
MTPAVASDYSGAPLGAPVYELTRVSKTYARNSVVALEDVDLTLRKGSFTSVIGSSGCGKS
TLLKIMAGLIPPSKGRVILQGEPVRGARRDIGMMFQQATLFPWKTAVENIVLPIEIRDGK
AAANKAMDKAYELLEIVGLKGFENVYPNELSGGMAQRASICRMLITEPAVLLLDEPFSAL
DELSRDMMNMELQRICREQNATAFLVTHSIQEAVILSDDIVVMKPRPGRIAEIVEVDLPR
PRTLDMMTTPKFGAIVDHIRGQLDKGEDM
Or try a new SitesBLAST search
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