SitesBLAST
Comparing HSERO_RS18940 FitnessBrowser__HerbieS:HSERO_RS18940 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)
51% identity, 100% coverage: 1:363/364 of query aligns to 1:371/372 of 1g291
- binding magnesium ion: D69 (= D73), E71 (= E75), K72 (vs. gap), K79 (= K77), D80 (≠ E78), Y228 (= Y226), D229 (≠ A227), E292 (= E289), D293 (≠ H290), S341 (≠ A333), E342 (≠ N334), K359 (≠ D351)
- binding pyrophosphate 2-: P37 (= P41), S38 (= S42), G39 (= G43), C40 (= C44), G41 (= G45), K42 (= K46), T43 (≠ S47), T44 (= T48)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
49% identity, 98% coverage: 1:355/364 of query aligns to 4:366/375 of 2d62A
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)
48% identity, 99% coverage: 1:359/364 of query aligns to 1:383/393 of P9WQI3
- H193 (= H196) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprC ABC transporter, ATP-binding protein SugC (see paper)
50% identity, 98% coverage: 2:356/364 of query aligns to 1:353/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S42), G39 (= G43), C40 (= C44), G41 (= G45), K42 (= K46), S43 (= S47), T44 (= T48), Q82 (= Q86), G132 (≠ R136), Q133 (= Q137), L134 (= L138), S135 (= S139), G136 (= G140), G137 (= G141), Q138 (= Q142), H192 (= H196)
- binding magnesium ion: S43 (= S47), Q82 (= Q86)
8hprD ABC transporter, ATP-binding protein SugC (see paper)
50% identity, 98% coverage: 2:356/364 of query aligns to 1:352/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y13), S38 (= S42), C40 (= C44), G41 (= G45), K42 (= K46), S43 (= S47), T44 (= T48), Q82 (= Q86), R129 (= R133), G132 (≠ R136), Q133 (= Q137), S135 (= S139), G136 (= G140), G137 (= G141), Q138 (= Q142), Q159 (≠ E163), H192 (= H196)
- binding magnesium ion: S43 (= S47), Q82 (= Q86), D158 (= D162)
8hplC ABC transporter, ATP-binding protein SugC (see paper)
47% identity, 98% coverage: 2:359/364 of query aligns to 1:377/384 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)
49% identity, 100% coverage: 1:363/364 of query aligns to 1:363/369 of P19566
- L86 (= L90) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P164) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D169) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E310) mutation to 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)
48% identity, 100% coverage: 1:363/364 of query aligns to 1:365/371 of P68187
- A85 (= A89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A121) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G128) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G141) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D162) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ T232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L245) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ L268) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G279) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ I283) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G285) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ L304) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E310) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ G324) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G340) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ S346) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F355) mutation to 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)
48% identity, 99% coverage: 2:363/364 of query aligns to 1:364/374 of 2awnB
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
48% identity, 99% coverage: 2:363/364 of query aligns to 1:364/372 of 2awoA
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
48% identity, 99% coverage: 2:363/364 of query aligns to 1:364/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), V17 (= V22), P36 (= P41), S37 (= S42), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), Q81 (= Q86), R128 (= R133), A132 (≠ Q137), S134 (= S139), G135 (= G140), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S47), Q81 (= Q86), D157 (= D162)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
48% identity, 99% coverage: 2:363/364 of query aligns to 1:364/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V22), S37 (= S42), G38 (= G43), C39 (= C44), G40 (= G45), K41 (= K46), S42 (= S47), T43 (= T48), R128 (= R133), A132 (≠ Q137), L133 (= L138), S134 (= S139), Q137 (= Q142)
- binding beryllium trifluoride ion: S37 (= S42), G38 (= G43), K41 (= K46), Q81 (= Q86), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S47), Q81 (= Q86), D157 (= D162)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
48% identity, 99% coverage: 2:363/364 of query aligns to 1:364/371 of 3puwA