SitesBLAST
Comparing BWI76_RS05870 FitnessBrowser__Koxy:BWI76_RS05870 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 86% coverage: 4:216/247 of query aligns to 15:228/378 of P69874
- C26 (≠ S15) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ W16) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L34) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C43) mutation to T: Loss of ATPase activity and transport.
- L60 (= L49) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I65) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 92% coverage: 7:233/247 of query aligns to 4:233/369 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 92% coverage: 7:233/247 of query aligns to 1:230/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (= W16), S35 (= S41), G36 (= G42), C37 (= C43), G38 (= G44), K39 (= K45), S40 (= S46), T41 (= T47), R126 (≠ A129), A130 (≠ Q133), S132 (= S135), G134 (= G137), Q135 (≠ M138)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 92% coverage: 7:233/247 of query aligns to 3:232/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 92% coverage: 7:233/247 of query aligns to 4:233/371 of P68187
- A85 (≠ R85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S124) 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 (= R228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
42% identity, 92% coverage: 7:233/247 of query aligns to 3:232/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (= W16), S37 (= S41), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), Q81 (= Q82), R128 (≠ A129), A132 (≠ Q133), S134 (= S135), G136 (= G137), Q137 (≠ M138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 92% coverage: 7:233/247 of query aligns to 3:232/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (= W16), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (≠ A129), S134 (= S135), Q137 (≠ M138)
- binding beryllium trifluoride ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 92% coverage: 7:233/247 of query aligns to 3:232/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (= W16), V17 (≠ A21), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (≠ A129), A132 (≠ Q133), S134 (= S135), Q137 (≠ M138)
- binding tetrafluoroaluminate ion: S37 (= S41), G38 (= G42), K41 (= K45), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 92% coverage: 7:233/247 of query aligns to 3:232/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (= W16), V17 (≠ A21), G38 (= G42), C39 (= C43), G40 (= G44), K41 (= K45), S42 (= S46), T43 (= T47), R128 (≠ A129), A132 (≠ Q133), S134 (= S135), Q137 (≠ M138)
- binding magnesium ion: S42 (= S46), Q81 (= Q82)
8hprC Lpqy-sugabc in state 4 (see paper)
44% identity, 79% coverage: 12:207/247 of query aligns to 8:207/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ W16), S38 (= S41), G39 (= G42), G41 (= G44), K42 (= K45), S43 (= S46), Q82 (= Q82), Q133 (= Q133), G136 (= G136), G137 (= G137), Q138 (≠ M138), H192 (= H192)
- binding magnesium ion: S43 (= S46), Q82 (= Q82)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
39% identity, 82% coverage: 7:208/247 of query aligns to 7:217/375 of 2d62A
8hprD Lpqy-sugabc in state 4 (see paper)
44% identity, 79% coverage: 12:207/247 of query aligns to 8:207/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ W16), S38 (= S41), C40 (= C43), G41 (= G44), K42 (= K45), S43 (= S46), T44 (= T47), Q82 (= Q82), R129 (≠ A129), Q133 (= Q133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (= S46), 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)
43% identity, 80% coverage: 11:207/247 of query aligns to 8:208/393 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.
8hplC Lpqy-sugabc in state 1 (see paper)
44% identity, 79% coverage: 12:207/247 of query aligns to 8:205/384 of 8hplC
1g291 Malk (see paper)
40% identity, 80% coverage: 12:208/247 of query aligns to 9:214/372 of 1g291
- binding magnesium ion: D69 (≠ E68), E71 (≠ V70), K72 (≠ T71), K79 (= K75), D80 (≠ E76)
- binding pyrophosphate 2-: S38 (= S41), G39 (= G42), C40 (= C43), G41 (= G44), K42 (= K45), T43 (≠ S46), T44 (= T47)
Sites not aligning to the query:
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
41% identity, 81% coverage: 9:207/247 of query aligns to 10:215/226 of 5xu1B
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
39% identity, 91% coverage: 11:236/247 of query aligns to 8:235/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ W16), Q14 (= Q17), T16 (≠ V19), V18 (≠ A21), S38 (= S41), G39 (= G42), C40 (= C43), G41 (= G44), K42 (= K45), T43 (≠ S46), T44 (= T47), R133 (≠ A129), E137 (≠ Q133), S139 (= S135), G141 (= G137), Q142 (≠ M138)
- binding calcium ion: T43 (≠ S46), Q86 (= Q82)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 78% coverage: 26:217/247 of query aligns to 46:244/382 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
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
38% identity, 78% coverage: 26:217/247 of query aligns to 46:244/382 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
7ahdC Opua (e190q) occluded (see paper)
37% identity, 78% coverage: 26:217/247 of query aligns to 46:244/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S41), G62 (= G42), G64 (= G44), K65 (= K45), S66 (= S46), T67 (= T47), Q111 (= Q82), K161 (≠ A132), Q162 (= Q133), S164 (= S135), G166 (= G137), M167 (= M138), Q188 (≠ E159), H221 (= H192)
Sites not aligning to the query:
Query Sequence
>BWI76_RS05870 FitnessBrowser__Koxy:BWI76_RS05870
MTSSTLVSFRHVRKSWQQVTALQNFSLDIAAGELVALVGSSGCGKSTLLRMLVGLESATQ
GEIRINGEPVTGVGKERGIVFQEPRLFPWLNVLDNVMLGLADEKLSRAAKRQRALEMLER
VQLSEFANALPAQLSGGMAQRVAIARGLVARPQILMLDEPFGALDALTRHTLQQELLQIH
QRAGTTTLLVTHDVEEAVALADRVVVLSPRPGRIREVVSLALPHPRQRDDASFSAACRQI
RNLITTA
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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