SitesBLAST
Comparing BPHYT_RS10405 FitnessBrowser__BFirm:BPHYT_RS10405 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 66% coverage: 29:224/298 of query aligns to 32:228/378 of P69874
- F45 (= F42) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C51) mutation to T: Loss of ATPase activity and transport.
- L60 (= L57) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V73) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V129) mutation to M: Loss of ATPase activity and transport.
- D172 (= D166) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 63% coverage: 27:215/298 of query aligns to 19:216/375 of 2d62A
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
36% identity, 72% coverage: 10:224/298 of query aligns to 2:225/232 of 1f3oA
8hplC Lpqy-sugabc in state 1 (see paper)
38% identity, 67% coverage: 15:215/298 of query aligns to 8:205/384 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)
39% identity, 68% coverage: 14:215/298 of query aligns to 8:208/393 of P9WQI3
- H193 (= H200) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 73% coverage: 9:225/298 of query aligns to 2:214/374 of 2awnB
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
36% identity, 72% coverage: 10:224/298 of query aligns to 2:225/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (= Y19), S40 (= S49), G41 (= G50), S42 (≠ C51), G43 (= G52), K44 (= K53), S45 (= S54), T46 (= T55), F138 (= F134), Q145 (= Q141), S147 (= S143), G149 (= G145), Q150 (≠ M146), H204 (= H200)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 73% coverage: 9:225/298 of query aligns to 3:215/371 of P68187
- A85 (≠ R93) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V122) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ H125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G127) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K132) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G145) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D166) 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.
1g291 Malk (see paper)
40% identity, 62% coverage: 32:215/298 of query aligns to 21:213/372 of 1g291
- binding magnesium ion: D69 (= D80), E71 (= E84), K72 (≠ R85), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S49), G39 (= G50), C40 (= C51), G41 (= G52), K42 (= K53), T43 (≠ S54), T44 (= T55)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 67% coverage: 27:225/298 of query aligns to 13:212/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S49), G36 (= G50), C37 (= C51), G38 (= G52), K39 (= K53), S40 (= S54), T41 (= T55), R126 (≠ S137), A130 (≠ Q141), S132 (= S143), G134 (= G145), Q135 (≠ M146)
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
39% identity, 73% coverage: 9:225/298 of query aligns to 2:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y19), S37 (= S49), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), Q81 (= Q90), R128 (≠ S137), A132 (≠ Q141), S134 (= S143), G136 (= G145), Q137 (≠ M146), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 73% coverage: 9:225/298 of query aligns to 2:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (≠ S137), S134 (= S143), Q137 (≠ M146)
- binding beryllium trifluoride ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q90), S134 (= S143), G136 (= G145), H191 (= H200)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 73% coverage: 9:225/298 of query aligns to 2:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), V17 (= V29), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (≠ S137), A132 (≠ Q141), S134 (= S143), Q137 (≠ M146)
- binding tetrafluoroaluminate ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q90), S134 (= S143), G135 (= G144), G136 (= G145), E158 (= E167), H191 (= H200)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 73% coverage: 9:225/298 of query aligns to 2:214/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y19), V17 (= V29), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (= S54), T43 (= T55), R128 (≠ S137), A132 (≠ Q141), S134 (= S143), Q137 (≠ M146)
- binding magnesium ion: S42 (= S54), Q81 (= Q90)
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 63% coverage: 28:215/298 of query aligns to 17:207/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S49), C40 (= C51), G41 (= G52), K42 (= K53), S43 (= S54), T44 (= T55), Q82 (= Q90), R129 (≠ S137), Q133 (= Q141), S135 (= S143), G136 (= G144), G137 (= G145), Q159 (≠ E167), H192 (= H200)
- binding magnesium ion: S43 (= S54), Q82 (= Q90)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 63% coverage: 28:215/298 of query aligns to 17:207/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S49), G39 (= G50), G41 (= G52), K42 (= K53), S43 (= S54), Q82 (= Q90), Q133 (= Q141), G136 (= G144), G137 (= G145), Q138 (≠ M146), H192 (= H200)
- binding magnesium ion: S43 (= S54), Q82 (= Q90)
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)
41% identity, 67% coverage: 27:225/298 of query aligns to 16:215/369 of P19566
- L86 (= L94) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P168) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D173) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
34% identity, 72% coverage: 10:225/298 of query aligns to 3:244/382 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
7aheC Opua inhibited inward facing (see paper)
34% identity, 72% coverage: 10:225/298 of query aligns to 3:244/382 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
3c4jA Abc protein artp in complex with atp-gamma-s
42% identity, 66% coverage: 18:215/298 of query aligns to 7:211/242 of 3c4jA
Query Sequence
>BPHYT_RS10405 FitnessBrowser__BFirm:BPHYT_RS10405
MTSSTLSDNIDILHVSKHYAQQGGTPLAVLDDISLRMRAGEFVSVLGSSGCGKSTLLRLI
AGLDTDYSGEIVVAGDQVRDTSLERGIVFQDHRLFPWLTASQNILAALRNAPLSAREKRE
AVAEHIGLVGLKGFENSYPHQLSGGMAQRVAIARGLVNRPRVLLLDEPFGALDALTRGRL
QNELQRIWEHERITMILVTHDVDEALYLGDRVVTMAPRPGRIKRIVDVALPRPRERNDPR
FIRLRDEVLADFVGHDGARREPRVDRDGRGDDEPHDGTRIPVVSPPVSPPITEWRLAW
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