SitesBLAST
Comparing BPHYT_RS21720 FitnessBrowser__BFirm:BPHYT_RS21720 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 75% coverage: 16:217/271 of query aligns to 34:241/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12
7aheC Opua inhibited inward facing (see paper)
38% identity, 75% coverage: 16:217/271 of query aligns to 34:241/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
42% identity, 73% coverage: 23:219/271 of query aligns to 31:228/378 of P69874
- F45 (= F37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V124) mutation to M: Loss of ATPase activity and transport.
- D172 (= D161) 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.
7ahdC Opua (e190q) occluded (see paper)
38% identity, 75% coverage: 16:217/271 of query aligns to 34:241/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (= T21), S61 (= S44), G62 (= G45), G64 (= G47), K65 (= K48), S66 (≠ T49), T67 (= T50), Q111 (= Q85), K161 (≠ Y135), Q162 (= Q136), S164 (= S138), G166 (= G140), M167 (= M141), Q188 (≠ E162), H221 (= H195)
Sites not aligning to the query:
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
39% identity, 76% coverage: 12:218/271 of query aligns to 9:221/226 of 5xu1B
3d31A Modbc from methanosarcina acetivorans (see paper)
38% identity, 69% coverage: 24:210/271 of query aligns to 15:201/348 of 3d31A
Sites not aligning to the query:
1g291 Malk (see paper)
38% identity, 70% coverage: 22:211/271 of query aligns to 16:214/372 of 1g291
- binding magnesium ion: D69 (≠ G75), E71 (≠ G77), K72 (≠ A78), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (= T49), T44 (= T50)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 70% coverage: 22:211/271 of query aligns to 19:217/375 of 2d62A
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
40% identity, 68% coverage: 27:210/271 of query aligns to 20:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), Q81 (= Q85), R128 (≠ F129), A132 (≠ M133), S134 (= S138), G136 (= G140), Q137 (≠ M141), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q85)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 68% coverage: 27:210/271 of query aligns to 20:206/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (≠ F129), S134 (= S138), Q137 (≠ M141)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S138), G136 (= G140), H191 (= H195)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q85)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 68% coverage: 27:210/271 of query aligns to 20:206/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (≠ F129), A132 (≠ M133), S134 (= S138), Q137 (≠ M141)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H195)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q85)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 68% coverage: 27:210/271 of query aligns to 20:206/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (≠ F129), A132 (≠ M133), S134 (= S138), Q137 (≠ M141)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q85)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 68% coverage: 27:210/271 of query aligns to 20:206/374 of 2awnB
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
40% identity, 68% coverage: 27:210/271 of query aligns to 21:207/371 of P68187
- A85 (= A88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ R114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D161) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 68% coverage: 27:210/271 of query aligns to 18:204/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (≠ T49), T41 (= T50), R126 (≠ F129), A130 (≠ M133), S132 (= S138), G134 (= G140), Q135 (≠ M141)
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)
36% identity, 77% coverage: 1:210/271 of query aligns to 1:207/369 of P19566
- L86 (= L89) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P163) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D168) 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 77% coverage: 1:210/271 of query aligns to 1:214/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 77% coverage: 1:210/271 of query aligns to 1:214/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 77% coverage: 1:210/271 of query aligns to 1:214/353 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)
36% identity, 77% coverage: 1:210/271 of query aligns to 1:214/353 of Q97UY8
- S142 (= S138) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G140) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E162) 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+).
Query Sequence
>BPHYT_RS21720 FitnessBrowser__BFirm:BPHYT_RS21720
MENMTVRNVSVVFPGRRPGQTVQALDDINLTIRSGDFVVALGASGCGKTTLLSLMAGFIA
PSRGELLLGGEPIAGPGADRGVVFQKHALLPWLNVIDNAEFGLKLQGVPRAQRREIAVRN
LALVGLQDFHKHMIYQLSGGMQQRVGIARALTCDPAMLLMDEPMAALDALTRETIQELLL
DVWKKTNKMFFFITHSVEEALFLASRLIVMSPRPGRITHTYELDFNRRFLESRDARAIKS
SPDFIAMREQVLNIIYGDEKMHAAEAGVAHV
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