SitesBLAST
Comparing H281DRAFT_00837 FitnessBrowser__Burk376:H281DRAFT_00837 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
39% identity, 70% coverage: 28:216/270 of query aligns to 42:239/382 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)
39% identity, 70% coverage: 28:216/270 of query aligns to 42:239/382 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)
39% identity, 70% coverage: 27:216/270 of query aligns to 41:239/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (≠ T47), G62 (= G48), G64 (= G50), K65 (= K51), S66 (= S52), T67 (= T53), Q111 (= Q88), K161 (≠ H138), Q162 (= Q139), S164 (= S141), G166 (= G143), M167 (= M144), Q188 (≠ E165), H221 (= H198)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 68% coverage: 33:216/270 of query aligns to 38:224/378 of P69874
- F45 (= F40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V127) mutation to M: Loss of ATPase activity and transport.
- D172 (= D164) 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.
8hprC Lpqy-sugabc in state 4 (see paper)
39% identity, 79% coverage: 4:216/270 of query aligns to 1:210/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F15), S38 (≠ T47), G39 (= G48), G41 (= G50), K42 (= K51), S43 (= S52), Q82 (= Q88), Q133 (= Q139), G136 (= G142), G137 (= G143), Q138 (≠ M144), H192 (= H198)
- binding magnesium ion: S43 (= S52), Q82 (= Q88)
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 79% coverage: 4:216/270 of query aligns to 1:210/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F15), S38 (≠ T47), C40 (= C49), G41 (= G50), K42 (= K51), S43 (= S52), T44 (= T53), Q82 (= Q88), R129 (= R135), Q133 (= Q139), S135 (= S141), G136 (= G142), G137 (= G143), Q159 (≠ E165), H192 (= H198)
- binding magnesium ion: S43 (= S52), Q82 (= Q88)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 71% coverage: 26:216/270 of query aligns to 20:219/375 of 2d62A
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)
40% identity, 71% coverage: 25:216/270 of query aligns to 17:211/393 of P9WQI3
- H193 (= H198) 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)
41% identity, 70% coverage: 27:216/270 of query aligns to 16:208/384 of 8hplC
Sites not aligning to the query:
1g291 Malk (see paper)
37% identity, 71% coverage: 26:216/270 of query aligns to 17:216/372 of 1g291
- binding magnesium ion: D69 (≠ E74), E71 (≠ L76), K72 (= K77), K79 (vs. gap), D80 (≠ N80)
- binding pyrophosphate 2-: S38 (≠ T47), G39 (= G48), C40 (= C49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53)
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
35% identity, 79% coverage: 3:216/270 of query aligns to 1:214/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (= F15), Q14 (= Q23), T16 (≠ Y25), V18 (≠ A27), S38 (≠ T47), G39 (= G48), C40 (= C49), G41 (= G50), K42 (= K51), T43 (≠ S52), T44 (= T53), R133 (= R135), E137 (≠ Q139), S139 (= S141), G141 (= G143), Q142 (≠ M144)
- binding calcium ion: T43 (≠ S52), Q86 (= Q88)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 79% coverage: 4:216/270 of query aligns to 1:209/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 79% coverage: 3:216/270 of query aligns to 1:210/371 of P68187
- A85 (= A91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ W123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ K125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G130) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G143) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D164) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
37% identity, 79% coverage: 4:216/270 of query aligns to 1:209/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F15), S37 (≠ T47), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), Q81 (= Q88), R128 (= R135), A132 (≠ Q139), S134 (= S141), G136 (= G143), Q137 (≠ M144), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S52), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 79% coverage: 4:216/270 of query aligns to 1:209/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F15), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R135), S134 (= S141), Q137 (≠ M144)
- binding beryllium trifluoride ion: S37 (≠ T47), G38 (= G48), K41 (= K51), Q81 (= Q88), S134 (= S141), G136 (= G143), H191 (= H198)
- binding magnesium ion: S42 (= S52), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 79% coverage: 4:216/270 of query aligns to 1:209/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (≠ A27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R135), A132 (≠ Q139), S134 (= S141), Q137 (≠ M144)
- binding tetrafluoroaluminate ion: S37 (≠ T47), G38 (= G48), K41 (= K51), Q81 (= Q88), S134 (= S141), G135 (= G142), G136 (= G143), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S52), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 79% coverage: 4:216/270 of query aligns to 1:209/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F15), V17 (≠ A27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (= S52), T43 (= T53), R128 (= R135), A132 (≠ Q139), S134 (= S141), Q137 (≠ M144)
- binding magnesium ion: S42 (= S52), Q81 (= Q88)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 70% coverage: 29:216/270 of query aligns to 17:207/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (≠ T47), G36 (= G48), C37 (= C49), G38 (= G50), K39 (= K51), S40 (= S52), T41 (= T53), R126 (= R135), A130 (≠ Q139), S132 (= S141), G134 (= G143), Q135 (≠ M144)
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)
38% identity, 70% coverage: 29:216/270 of query aligns to 20:210/369 of P19566
- L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P166) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D171) 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.
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
35% identity, 78% coverage: 6:216/270 of query aligns to 4:218/226 of 5xu1B
Query Sequence
>H281DRAFT_00837 FitnessBrowser__Burk376:H281DRAFT_00837
MTVAALALENITCTFAARDNRAQRYTAVKDTTLRIAPGEFVSVVGPTGCGKSTLLNVGAG
LLGPSSGSVSVFGEPLKGINRRAGYMFQADALMPWRSAIDNVLAGLAFHGVPQAEAREKA
DEWLKRVGLGGFGDRYPHQLSGGMRKRVAMAQTLILDPDIILMDEPFSALDIQTRQLMEN
ELLELWAAKRKAVLFITHDLDEAIAMSDRVVVLSAGPGTHPIGEFTIDLPRPRDVAEIRS
HPRFVELHAQIWSVLRDEVLKGYQQQLSAV
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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