SitesBLAST
Comparing BPHYT_RS11215 FitnessBrowser__BFirm:BPHYT_RS11215 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
41% identity, 94% coverage: 11:508/532 of query aligns to 3:491/501 of P04983
- K43 (= K50) mutation to R: Loss of transport.
7arlD Lolcde in complex with lipoprotein and adp (see paper)
33% identity, 41% coverage: 12:231/532 of query aligns to 2:221/222 of 7arlD
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
33% identity, 41% coverage: 12:231/532 of query aligns to 5:224/233 of P75957
- G42 (= G44) mutation to D: Loss of lipoprotein release when overexpressed.
7mdyC Lolcde nucleotide-bound
33% identity, 41% coverage: 12:231/532 of query aligns to 2:221/226 of 7mdyC
- binding adp orthovanadate: Y12 (= Y22), G42 (= G47), S43 (≠ A48), G44 (= G49), K45 (= K50), S46 (= S51), T47 (= T52), Q91 (= Q93), H138 (≠ T148), E142 (= E152), S144 (≠ G154), G145 (≠ I155), G146 (= G156), E168 (= E178), N172 (≠ M182), H201 (= H210)
- binding magnesium ion: S46 (= S51), Q91 (= Q93)
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
32% identity, 41% coverage: 12:231/532 of query aligns to 4:223/229 of 7v8iD
- binding phosphoaminophosphonic acid-adenylate ester: V23 (= V26), S43 (≠ N46), G44 (= G47), G46 (= G49), K47 (= K50), S48 (= S51), T49 (= T52), Q93 (= Q93), R137 (≠ D145), H140 (≠ T148), E144 (= E152), S146 (≠ G154), G148 (= G156), E149 (≠ H157), H203 (= H210)
- binding magnesium ion: S48 (= S51), Q93 (= Q93)
P07821 Iron(3+)-hydroxamate import ATP-binding protein FhuC; Ferric hydroxamate uptake protein C; Ferrichrome transport ATP-binding protein FhuC; Iron(III)-hydroxamate import ATP-binding protein FhuC; EC 7.2.2.16 from Escherichia coli (strain K12) (see 2 papers)
33% identity, 43% coverage: 26:254/532 of query aligns to 26:250/265 of P07821
- K50 (= K50) mutation to Q: Lack of activity.
- D172 (= D177) mutation to E: Lack of activity.
- E173 (= E178) mutation to A: Lack of activity.
7w78A Heme exporter hrtba in complex with mg-amppnp (see paper)
33% identity, 41% coverage: 12:229/532 of query aligns to 4:214/218 of 7w78A
7w79A Heme exporter hrtba in complex with mn-amppnp (see paper)
33% identity, 41% coverage: 12:229/532 of query aligns to 4:214/216 of 7w79A
- binding adenosine-5'-triphosphate: Y14 (= Y22), S43 (≠ N46), G44 (= G47), S45 (≠ A48), G46 (= G49), K47 (= K50), S48 (= S51), T49 (= T52)
- binding manganese (ii) ion: S6 (= S14), E30 (≠ S33), S48 (= S51), Q88 (= Q93), E163 (= E178), H196 (= H210)
5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
32% identity, 39% coverage: 26:231/532 of query aligns to 22:221/615 of 5lilA
- binding adenosine-5'-triphosphate: V22 (= V26), S42 (≠ N46), G43 (= G47), G45 (= G49), K46 (= K50), S47 (= S51), T48 (= T52), Q92 (= Q93), K136 (vs. gap), Q143 (≠ T148), S145 (≠ V150), G147 (= G156), Q148 (≠ H157)
- binding magnesium ion: S47 (= S51), Q92 (= Q93)
Sites not aligning to the query:
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
32% identity, 39% coverage: 26:231/532 of query aligns to 22:221/592 of 5lj7A
- binding adenosine-5'-triphosphate: V22 (= V26), S42 (≠ N46), G43 (= G47), G45 (= G49), K46 (= K50), S47 (= S51), T48 (= T52), Q92 (= Q93), K136 (vs. gap), Q143 (≠ T148), S145 (≠ V150), G147 (= G156), Q148 (≠ H157)
- binding magnesium ion: S47 (= S51), Q92 (= Q93)
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
26% identity, 41% coverage: 12:231/532 of query aligns to 4:229/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
26% identity, 41% coverage: 12:231/532 of query aligns to 4:229/253 of 1g9xB
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, 45% coverage: 11:250/532 of query aligns to 2:235/369 of P19566
- L86 (= L97) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P179) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ T184) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
32% identity, 45% coverage: 11:250/532 of query aligns to 1:234/374 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)
32% identity, 45% coverage: 11:250/532 of query aligns to 1:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y22), S37 (≠ N46), G38 (= G47), C39 (≠ A48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), Q81 (= Q93), R128 (≠ A143), A132 (≠ T148), S134 (≠ V150), G136 (= G156), Q137 (≠ H157), E158 (= E178), H191 (= H210)
- binding magnesium ion: S42 (= S51), Q81 (= Q93)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
32% identity, 45% coverage: 11:250/532 of query aligns to 1:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), G38 (= G47), C39 (≠ A48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ A143), S134 (≠ V150), Q137 (≠ H157)
- binding beryllium trifluoride ion: S37 (≠ N46), G38 (= G47), K41 (= K50), Q81 (= Q93), S134 (≠ V150), G136 (= G156), H191 (= H210)
- binding magnesium ion: S42 (= S51), Q81 (= Q93)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
32% identity, 45% coverage: 11:250/532 of query aligns to 1:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), V17 (≠ L27), G38 (= G47), C39 (≠ A48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ A143), A132 (≠ T148), S134 (≠ V150), Q137 (≠ H157)
- binding tetrafluoroaluminate ion: S37 (≠ N46), G38 (= G47), K41 (= K50), Q81 (= Q93), S134 (≠ V150), G135 (= G151), G136 (= G156), E158 (= E178), H191 (= H210)
- binding magnesium ion: S42 (= S51), Q81 (= Q93)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
32% identity, 45% coverage: 11:250/532 of query aligns to 1:234/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y22), V17 (≠ L27), G38 (= G47), C39 (≠ A48), G40 (= G49), K41 (= K50), S42 (= S51), T43 (= T52), R128 (≠ A143), A132 (≠ T148), S134 (≠ V150), Q137 (≠ H157)
- binding magnesium ion: S42 (= S51), Q81 (= Q93)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 45% coverage: 11:250/532 of query aligns to 2:235/371 of P68187
- A85 (≠ N96) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ L128) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ M136) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V139) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (vs. gap) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G156) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D177) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E243) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
29% identity, 46% coverage: 12:255/532 of query aligns to 6:243/353 of 1oxvD
Query Sequence
>BPHYT_RS11215 FitnessBrowser__BFirm:BPHYT_RS11215
MDSTDHDAVPAVLSVSGIGKTYAEPVLADISLSLRAGEVLALTGENGAGKSTLSKIIGGL
VEPTAGTMQLGGVPYAPASRTQAEALGVRMVMQELNLLPTLSVAENLFLNRLPRAGAFSF
GWIDRRKLREDARQAMAQVGLDAIDPDTLVGELGIGHQQMVEIARNLIDDCRVLILDEPT
AMLTAREVDLLFEQIDRLKARGVALVYISHRLEELARVAEQIAVLRDGRLVHVDAMANLT
SDEIVTWMVGRELGERIDLGVRNIGAPLLKVDRLTRGKVVREVSFEVRAGEIFGISGLIG
AGRTELMRLIYGADPKDSGTVSLAATPGAPPTPVQIASPSDAVRAGIALITEDRKGEGLL
LPQPIAANVSLGNIGSVARHGIVDAKRENALAQTQIAAMRIRTSGPGQIVGELSGGNQQK
VVIGRWLARDCRVLLFDEPTRGIDVGAKFDIYGLMGALAREGRALVVVSSDLRELMLICD
RIGVMSAGSMTGVFERDNWSQDALLAAAFAGYRSREALLHAAPDTSEAGSAS
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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