SitesBLAST
Comparing Pf6N2E2_2777 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2777 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)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 84% coverage: 1:219/262 of query aligns to 1:212/371 of P68187
- A85 (≠ S83) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A121) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L124) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D126) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G131) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G144) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) 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.
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, 84% coverage: 1:219/262 of query aligns to 1:212/369 of P19566
- L86 (≠ V84) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D172) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
38% identity, 82% coverage: 4:219/262 of query aligns to 3:211/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q80), R128 (≠ K136), A132 (≠ Q140), S134 (= S142), G136 (= G144), Q137 (≠ M145), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (= S43), Q81 (= Q80)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 82% coverage: 4:219/262 of query aligns to 3:211/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (≠ K136), S134 (= S142), Q137 (≠ M145)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q80), S134 (= S142), G136 (= G144), H191 (= H199)
- binding magnesium ion: S42 (= S43), Q81 (= Q80)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 82% coverage: 4:219/262 of query aligns to 3:211/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (≠ K136), A132 (≠ Q140), S134 (= S142), Q137 (≠ M145)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q80), S134 (= S142), G135 (= G143), G136 (= G144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (= S43), Q81 (= Q80)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 82% coverage: 4:219/262 of query aligns to 3:211/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y13), V17 (= V18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), R128 (≠ K136), A132 (≠ Q140), S134 (= S142), Q137 (≠ M145)
- binding magnesium ion: S42 (= S43), Q81 (= Q80)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 82% coverage: 4:219/262 of query aligns to 3:211/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 82% coverage: 4:219/262 of query aligns to 1:209/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y13), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (= S43), T41 (= T44), R126 (≠ K136), A130 (≠ Q140), S132 (= S142), G134 (= G144), Q135 (≠ M145)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
36% identity, 82% coverage: 1:216/262 of query aligns to 4:218/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 84% coverage: 18:238/262 of query aligns to 32:241/378 of P69874
- F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ Q116) mutation to M: Loss of ATPase activity and transport.
- D172 (= D165) 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.
1g291 Malk (see paper)
36% identity, 82% coverage: 1:216/262 of query aligns to 1:215/372 of 1g291
- binding magnesium ion: D69 (≠ E70), E71 (vs. gap), K72 (vs. gap), K79 (vs. gap), D80 (= D72)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (≠ S43), T44 (= T44)
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
37% identity, 81% coverage: 3:215/262 of query aligns to 1:210/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y13), V16 (= V18), S36 (= S38), G37 (= G39), S38 (≠ C40), G39 (= G41), K40 (= K42), S41 (= S43), T42 (= T44), E162 (= E166), H194 (= H199)
- binding magnesium ion: S41 (= S43), E162 (= E166)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
37% identity, 79% coverage: 7:214/262 of query aligns to 30:236/382 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)
37% identity, 79% coverage: 7:214/262 of query aligns to 30:236/382 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
38% identity, 82% coverage: 1:215/262 of query aligns to 1:212/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
38% identity, 82% coverage: 1:215/262 of query aligns to 1:212/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
38% identity, 82% coverage: 1:215/262 of query aligns to 1:212/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
38% identity, 82% coverage: 1:215/262 of query aligns to 1:212/242 of 2oljA
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)
36% identity, 82% coverage: 1:214/262 of query aligns to 1:208/393 of P9WQI3
- H193 (= H199) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
7ahdC Opua (e190q) occluded (see paper)
36% identity, 79% coverage: 7:214/262 of query aligns to 30:236/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ Q16), S61 (= S38), G62 (= G39), G64 (= G41), K65 (= K42), S66 (= S43), T67 (= T44), Q111 (= Q80), K161 (≠ A139), Q162 (= Q140), S164 (= S142), G166 (= G144), M167 (= M145), Q188 (≠ E166), H221 (= H199)
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_2777 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2777
MSFITVNNVWQQYADQVVLERLNLRVAEGEFCTLVGASGCGKSTFLRLLLGQERASRGQI
LLDGEPLAGEPDASRGVVFQRYSVFPHLSVLDNVTLGLELPRSALLGRLFGSAKRQAREE
AAQLLDKVGLGHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMH
ALLLELWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAPGAYGARITYDIPLNSD
RRTARAAVDALPAELAGTLRIA
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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