SitesBLAST
Comparing BPHYT_RS27960 FitnessBrowser__BFirm:BPHYT_RS27960 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
47% identity, 94% coverage: 1:344/367 of query aligns to 4:366/375 of 2d62A
8hprC Lpqy-sugabc in state 4 (see paper)
47% identity, 94% coverage: 4:349/367 of query aligns to 3:357/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (≠ T43), Q82 (= Q82), Q133 (≠ G133), G136 (= G136), G137 (= G137), Q138 (≠ D138), H192 (= H192)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q82)
8hprD Lpqy-sugabc in state 4 (see paper)
47% identity, 94% coverage: 4:349/367 of query aligns to 3:356/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (= S38), C40 (= C40), G41 (= G41), K42 (= K42), S43 (≠ T43), T44 (= T44), Q82 (= Q82), R129 (= R129), Q133 (≠ G133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q82)
1g291 Malk (see paper)
47% identity, 95% coverage: 1:350/367 of query aligns to 1:369/372 of 1g291
- binding magnesium ion: D69 (= D63), E71 (= E65), K72 (≠ D66), K79 (≠ R73), D80 (≠ Q74), E292 (= E281), D293 (≠ H282), K359 (≠ R340)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)
8hplC Lpqy-sugabc in state 1 (see paper)
54% identity, 76% coverage: 4:283/367 of query aligns to 3:284/384 of 8hplC
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)
45% identity, 95% coverage: 1:349/367 of query aligns to 1:384/393 of P9WQI3
- H193 (= H192) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
49% identity, 87% coverage: 1:320/367 of query aligns to 4:320/353 of 1vciA
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 83% coverage: 1:304/367 of query aligns to 1:313/371 of P68187
- A85 (= A85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ H119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ V228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (= F241) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ S263) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ A271) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ L275) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G277) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G293) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E299) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
Sites not aligning to the query:
- 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)
47% identity, 77% coverage: 1:283/367 of query aligns to 1:288/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D165) 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)
45% identity, 83% coverage: 2:304/367 of query aligns to 1:312/374 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)
45% identity, 83% coverage: 2:304/367 of query aligns to 1:312/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (≠ G133), S134 (= S135), G136 (= G137), Q137 (≠ D138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
45% identity, 83% coverage: 2:304/367 of query aligns to 1:312/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R129), S134 (= S135), Q137 (≠ D138)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
45% identity, 83% coverage: 2:304/367 of query aligns to 1:312/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R129), A132 (≠ G133), S134 (= S135), Q137 (≠ D138)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
45% identity, 83% coverage: 2:304/367 of query aligns to 1:312/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R129), A132 (≠ G133), S134 (= S135), Q137 (≠ D138)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
45% identity, 81% coverage: 6:303/367 of query aligns to 3:309/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F13), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (≠ T43), T41 (= T44), R126 (= R129), A130 (≠ G133), S132 (= S135), G134 (= G137), Q135 (≠ D138)
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 80% coverage: 12:303/367 of query aligns to 4:281/344 of 2awnC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 77% coverage: 4:287/367 of query aligns to 18:303/378 of P69874
- C26 (≠ R12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ A260) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E281) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
3d31A Modbc from methanosarcina acetivorans (see paper)
42% identity, 63% coverage: 4:235/367 of query aligns to 2:229/348 of 3d31A
Sites not aligning to the query:
2awnA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 83% coverage: 2:304/367 of query aligns to 1:270/330 of 2awnA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
32% identity, 95% coverage: 1:347/367 of query aligns to 1:353/353 of 1oxvD
Query Sequence
>BPHYT_RS27960 FitnessBrowser__BFirm:BPHYT_RS27960
MSTIVLANLHKRFDDFVAVRDTSLTIGAGRFVVLLGPSGCGKTTTLRMIAGLELPTSGQI
FIDGEDVTALRARQRDIAFVFQMFALYPHMTVRNNIAFPLKNEHVSRKEIAARVAAAAHM
LRIENILDRKTGGLSGGDRQRVALGRAIVRQPKAFLMDEPLGTLDADFRELMCLELRKLH
NALAATTVYVTHDQSEAMAMADDIVVMNKGELLQAGPPQEIYHFPATVFVGNFIGSPPMN
FLPVDGGVDAGQEEVHLHGAQISVPRCEAAAERVLLGIRPEHVTINQHGPLRGKVIADEY
LGSHQVLVVETALGVVRVRVGKDEGLPAGSPVGLSFRKERTLLYDAQSGRLLPGAARTVP
AQGEANG
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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