SitesBLAST
Comparing BPHYT_RS27955 FitnessBrowser__BFirm:BPHYT_RS27955 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
43% identity, 99% coverage: 1:342/345 of query aligns to 4:372/375 of 2d62A
1g291 Malk (see paper)
49% identity, 78% coverage: 1:268/345 of query aligns to 1:272/372 of 1g291
- binding magnesium ion: D69 (= D63), E71 (≠ G65), K72 (≠ I66), K79 (≠ S73), D80 (= D74)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (≠ A40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
52% identity, 71% coverage: 1:245/345 of query aligns to 1:243/369 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 (= P162) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D167) 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
50% identity, 71% coverage: 1:245/345 of query aligns to 1:243/371 of P68187
- A85 (≠ S85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V116) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V119) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E121) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E126) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G139) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D160) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L230) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L243) 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
50% identity, 71% coverage: 2:245/345 of query aligns to 1:242/374 of 2awnB
8hprD Lpqy-sugabc in state 4 (see paper)
46% identity, 78% coverage: 2:270/345 of query aligns to 1:279/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (= S38), C40 (≠ A40), G41 (= G41), K42 (= K42), S43 (≠ T43), T44 (= T44), Q82 (= Q82), R129 (≠ N131), Q133 (≠ H135), S135 (= S137), G136 (= G138), G137 (= G139), Q159 (≠ E161), H192 (= H194)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q82)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
50% identity, 71% coverage: 2:245/345 of query aligns to 1:242/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), S37 (= S38), G38 (= G39), C39 (≠ A40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), Q81 (= Q82), R128 (≠ N131), A132 (≠ H135), S134 (= S137), G136 (= G139), Q137 (≠ E140), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
50% identity, 71% coverage: 2:245/345 of query aligns to 1:242/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F13), G38 (= G39), C39 (≠ A40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (≠ N131), S134 (= S137), Q137 (≠ E140)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S137), G136 (= G139), H191 (= H194)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
50% identity, 71% coverage: 2:245/345 of query aligns to 1:242/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A18), G38 (= G39), C39 (≠ A40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (≠ N131), A132 (≠ H135), S134 (= S137), Q137 (≠ E140)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S137), G135 (= G138), G136 (= G139), E158 (= E161), H191 (= H194)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
50% identity, 71% coverage: 2:245/345 of query aligns to 1:242/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F13), V17 (≠ A18), G38 (= G39), C39 (≠ A40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (≠ N131), A132 (≠ H135), S134 (= S137), Q137 (≠ E140)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
8hprC Lpqy-sugabc in state 4 (see paper)
46% identity, 78% coverage: 2:270/345 of query aligns to 1:279/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (≠ T43), Q82 (= Q82), Q133 (≠ H135), G136 (= G138), G137 (= G139), Q138 (≠ E140), H192 (= H194)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q82)
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)
47% identity, 79% coverage: 1:273/345 of query aligns to 1:273/393 of P9WQI3
- H193 (= H194) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
50% identity, 70% coverage: 4:245/345 of query aligns to 1:240/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F13), S35 (= S38), G36 (= G39), C37 (≠ A40), G38 (= G41), K39 (= K42), S40 (≠ T43), T41 (= T44), R126 (≠ N131), A130 (≠ H135), S132 (= S137), G134 (= G139), Q135 (≠ E140)
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 78% coverage: 2:270/345 of query aligns to 1:277/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 71% coverage: 1:244/345 of query aligns to 4:237/353 of 1vciA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 80% coverage: 1:277/345 of query aligns to 1:290/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 80% coverage: 1:277/345 of query aligns to 1:290/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 80% coverage: 1:277/345 of query aligns to 1:290/353 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)
40% identity, 80% coverage: 1:277/345 of query aligns to 1:290/353 of Q97UY8
- S142 (= S137) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G139) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E161) 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+).
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 77% coverage: 4:268/345 of query aligns to 18:299/378 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 (≠ A40) 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 (≠ L123) mutation to M: Loss of ATPase activity and transport.
- D172 (= D160) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E266) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
Query Sequence
>BPHYT_RS27955 FitnessBrowser__BFirm:BPHYT_RS27955
MAEIQLRNVSKRFGDIVAVDDLSIDVMDGEFVVLLGPSGAGKTTTLRLIAGLERPDAGDV
LIDGGIATGVHPSDRDVAFIFQQYSLYPHLTVFGNLAFPLRSPRRRSSEAEVRARVHAVA
EMLHMESKLDNMATHLSGGEMQRVAIGRALVRQPKVFLMDEPLSSLDAKLREELRIELKR
LHRAIGATIIYVTHDQVEATTLADRIGILDQGRLVQLGTPREVYGNPVSLSAAQRLGSPP
INLLPPTLLNLAHIPAGTTTVAIRPEDIVLHDPDVGDARGVQDALNLTVLEYSPLRHLLI
LDRAGTAVVVTTVAERNFSPGQSVGVSLPARSLLYFRADGRRIPT
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