SitesBLAST
Comparing BPHYT_RS29175 FitnessBrowser__BFirm:BPHYT_RS29175 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)
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)
44% identity, 88% coverage: 49:390/390 of query aligns to 17:387/393 of P9WQI3
- H193 (= H225) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
45% identity, 89% coverage: 35:382/390 of query aligns to 5:366/375 of 2d62A
1g291 Malk (see paper)
45% identity, 88% coverage: 46:387/390 of query aligns to 13:368/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (= E98), K72 (≠ D99), K79 (= K106), D80 (= D107), E292 (= E319), D293 (= D320), K359 (≠ H378)
- binding pyrophosphate 2-: S38 (= S71), G39 (= G72), C40 (= C73), G41 (= G74), K42 (= K75), T43 (≠ S76), T44 (= T77)
8hprC Lpqy-sugabc in state 4 (see paper)
45% identity, 87% coverage: 52:390/390 of query aligns to 19:360/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S71), G39 (= G72), G41 (= G74), K42 (= K75), S43 (= S76), Q82 (= Q115), Q133 (= Q166), G136 (= G169), G137 (= G170), Q138 (= Q171), H192 (= H225)
- binding magnesium ion: S43 (= S76), Q82 (= Q115)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
45% identity, 87% coverage: 52:390/390 of query aligns to 19:359/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S71), C40 (= C73), G41 (= G74), K42 (= K75), S43 (= S76), T44 (= T77), Q82 (= Q115), R129 (= R162), Q133 (= Q166), S135 (= S168), G136 (= G169), G137 (= G170), Q159 (≠ E192), H192 (= H225)
- binding magnesium ion: S43 (= S76), Q82 (= Q115)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 87% coverage: 52:390/390 of query aligns to 17:381/384 of 8hplC
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
43% identity, 90% coverage: 35:384/390 of query aligns to 5:346/353 of 1vciA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
54% identity, 62% coverage: 35:275/390 of query aligns to 1:241/374 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)
54% identity, 62% coverage: 35:275/390 of query aligns to 1:241/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ L46), S37 (= S71), G38 (= G72), C39 (= C73), G40 (= G74), K41 (= K75), S42 (= S76), T43 (= T77), Q81 (= Q115), R128 (= R162), A132 (≠ Q166), S134 (= S168), G136 (= G170), Q137 (= Q171), E158 (= E192), H191 (= H225)
- binding magnesium ion: S42 (= S76), Q81 (= Q115)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
54% identity, 62% coverage: 35:275/390 of query aligns to 1:241/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ L46), G38 (= G72), C39 (= C73), G40 (= G74), K41 (= K75), S42 (= S76), T43 (= T77), R128 (= R162), S134 (= S168), Q137 (= Q171)
- binding beryllium trifluoride ion: S37 (= S71), G38 (= G72), K41 (= K75), Q81 (= Q115), S134 (= S168), G136 (= G170), H191 (= H225)
- binding magnesium ion: S42 (= S76), Q81 (= Q115)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
54% identity, 62% coverage: 35:275/390 of query aligns to 1:241/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ L46), V17 (= V51), G38 (= G72), C39 (= C73), G40 (= G74), K41 (= K75), S42 (= S76), T43 (= T77), R128 (= R162), A132 (≠ Q166), S134 (= S168), Q137 (= Q171)
- binding tetrafluoroaluminate ion: S37 (= S71), G38 (= G72), K41 (= K75), Q81 (= Q115), S134 (= S168), G135 (= G169), G136 (= G170), E158 (= E192), H191 (= H225)
- binding magnesium ion: S42 (= S76), Q81 (= Q115)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
54% identity, 62% coverage: 35:275/390 of query aligns to 1:241/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ L46), V17 (= V51), G38 (= G72), C39 (= C73), G40 (= G74), K41 (= K75), S42 (= S76), T43 (= T77), R128 (= R162), A132 (≠ Q166), S134 (= S168), Q137 (= Q171)
- binding magnesium ion: S42 (= S76), Q81 (= Q115)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
54% identity, 62% coverage: 35:275/390 of query aligns to 2:242/371 of P68187
- A85 (= A118) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P139) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V147) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A150) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E152) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G157) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G170) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D191) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L261) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L274) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
54% identity, 62% coverage: 35:275/390 of query aligns to 2:242/369 of P19566
- L86 (= L119) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P193) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D198) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
54% identity, 61% coverage: 37:275/390 of query aligns to 1:239/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ L46), S35 (= S71), G36 (= G72), C37 (= C73), G38 (= G74), K39 (= K75), S40 (= S76), T41 (= T77), R126 (= R162), A130 (≠ Q166), S132 (= S168), G134 (= G170), Q135 (= Q171)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
53% identity, 60% coverage: 43:275/390 of query aligns to 2:211/344 of 2awnC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
53% identity, 57% coverage: 51:272/390 of query aligns to 32:253/378 of P69874
- F45 (= F64) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C73) mutation to T: Loss of ATPase activity and transport.
- L60 (= L79) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I95) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L154) mutation to M: Loss of ATPase activity and transport.
- D172 (= D191) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
- 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.
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
44% identity, 62% coverage: 35:275/390 of query aligns to 1:199/330 of 2awnA
3d31A Modbc from methanosarcina acetivorans (see paper)
40% identity, 59% coverage: 49:279/390 of query aligns to 13:238/348 of 3d31A
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
32% identity, 81% coverage: 37:351/390 of query aligns to 4:308/353 of 1oxvD
Query Sequence
>BPHYT_RS29175 FitnessBrowser__BFirm:BPHYT_RS29175
MANMANAADMAGGVGVADVASSPDAADAAGLTNPANVAVRNLTIQLGANTVIENLDLDVQ
AGEFVVLLGPSGCGKSTLLHSIAGLIDVTDGSIEIAGEDMTWADPKDRRIALVFQSYALY
PTMSVERNLSFALRINGTPKAEIARRVARASEMLQLGPLLKRKPAQLSGGQRQRVAIGRA
IVREADVFLFDEPLSNLDAKLRTELRRELKQLHQRLGATMIYVTHDQVEAMTLATRMAVM
RGGVIQQFGTPAEVYARPDNLFVATFLGTPAMNLIKGRLETRDGALHFCTEHWRLDVSRY
PFRTTPANGLPCVLGVRAEDVRLAEGASEHAKVSLVEPMGNHRVIWLDYHGVQVASIDQT
KTPLAIGDAAAFSFDSTHVSLFDEAGGARL
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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