SitesBLAST
Comparing Pf6N2E2_1743 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1743 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)
46% identity, 80% coverage: 7:300/368 of query aligns to 10:301/378 of P69874
- C26 (≠ S23) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y24) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F43) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S52) mutation to T: Loss of ATPase activity and transport.
- L60 (= L58) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ M74) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V133) mutation to M: Loss of ATPase activity and transport.
- D172 (= D170) mutation to N: Loss of ATPase activity and transport.
- C276 (vs. gap) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E296) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
50% identity, 60% coverage: 26:247/368 of query aligns to 17:244/375 of 2d62A
1g291 Malk (see paper)
48% identity, 60% coverage: 26:247/368 of query aligns to 14:241/372 of 1g291
- binding magnesium ion: D69 (≠ K81), E71 (vs. gap), K72 (vs. gap), K79 (≠ H85), D80 (≠ Q86)
- binding pyrophosphate 2-: S38 (= S50), G39 (= G51), C40 (≠ S52), G41 (= G53), K42 (= K54), T43 (= T55), T44 (= T56)
Sites not aligning to the query:
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)
49% identity, 63% coverage: 15:247/368 of query aligns to 4:236/393 of P9WQI3
- H193 (= H204) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 95% coverage: 15:365/368 of query aligns to 4:353/369 of P19566
- L86 (= L98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P172) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D177) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ I316) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 95% coverage: 15:365/368 of query aligns to 3:354/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 95% coverage: 15:365/368 of query aligns to 4:355/371 of P68187
- A85 (= A97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ N118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A129) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D131) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ H136) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G149) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D170) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ A240) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (vs. gap) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ T275) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ P286) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ E290) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ V292) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ A310) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ I316) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ H330) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G350) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ D356) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F365) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 95% coverage: 15:365/368 of query aligns to 1:352/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y24), S35 (= S50), G36 (= G51), C37 (≠ S52), G38 (= G53), K39 (= K54), S40 (≠ T55), T41 (= T56), R126 (= R141), A130 (≠ E145), S132 (= S147), G134 (= G149), Q135 (= Q150)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 95% coverage: 15:365/368 of query aligns to 3:354/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y24), S37 (= S50), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), Q81 (= Q94), R128 (= R141), A132 (≠ E145), S134 (= S147), G136 (= G149), Q137 (= Q150), E158 (= E171), H191 (= H204)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 95% coverage: 15:365/368 of query aligns to 3:354/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y24), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R141), S134 (= S147), Q137 (= Q150)
- binding beryllium trifluoride ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S147), G136 (= G149), H191 (= H204)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 95% coverage: 15:365/368 of query aligns to 3:354/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y24), V17 (= V30), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R141), A132 (≠ E145), S134 (= S147), Q137 (= Q150)
- binding tetrafluoroaluminate ion: S37 (= S50), G38 (= G51), K41 (= K54), Q81 (= Q94), S134 (= S147), G135 (= G148), G136 (= G149), E158 (= E171), H191 (= H204)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 95% coverage: 15:365/368 of query aligns to 3:354/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y24), V17 (= V30), G38 (= G51), C39 (≠ S52), G40 (= G53), K41 (= K54), S42 (≠ T55), T43 (= T56), R128 (= R141), A132 (≠ E145), S134 (= S147), Q137 (= Q150)
- binding magnesium ion: S42 (≠ T55), Q81 (= Q94)
8hprC Lpqy-sugabc in state 4 (see paper)
42% identity, 77% coverage: 15:298/368 of query aligns to 3:286/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y24), S38 (= S50), G39 (= G51), G41 (= G53), K42 (= K54), S43 (≠ T55), Q82 (= Q94), Q133 (≠ E145), G136 (= G148), G137 (= G149), Q138 (= Q150), H192 (= H204)
- binding magnesium ion: S43 (≠ T55), Q82 (= Q94)
8hprD Lpqy-sugabc in state 4 (see paper)
42% identity, 77% coverage: 15:298/368 of query aligns to 3:286/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y24), S38 (= S50), C40 (≠ S52), G41 (= G53), K42 (= K54), S43 (≠ T55), T44 (= T56), Q82 (= Q94), R129 (= R141), Q133 (≠ E145), S135 (= S147), G136 (= G148), G137 (= G149), Q159 (≠ E171), H192 (= H204)
- binding magnesium ion: S43 (≠ T55), Q82 (= Q94)
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 77% coverage: 15:298/368 of query aligns to 3:284/384 of 8hplC
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
39% identity, 93% coverage: 26:366/368 of query aligns to 17:345/353 of 1vciA
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 91% coverage: 30:365/368 of query aligns to 10:324/344 of 2awnC
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 86% coverage: 14:329/368 of query aligns to 1:312/348 of 3d31A
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 72% coverage: 26:291/368 of query aligns to 16:283/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 72% coverage: 26:291/368 of query aligns to 16:283/353 of 1oxvA
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_1743 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1743
MNAKATRPQTTLPLIEFNGVQKSYDGKTLVIKDLNLAISRGEFLTLLGASGSGKTTTLMM
LAGFETPTRGEILMGGTPIQKKPAHQRGMGMVFQNYALFPHMSVEENLAYPLKMRGLNRS
DLQAKVKRAIDMVQLHGMQQRRITELSGGQQQRVALARAMVFEPEVILMDEPLGALDKNL
REHMQYEIKQLHKSLGVTVVYVTHDQSEALTMSDRIAVFHEGDIAQIGSPTALYEHPENA
YVANFIGENNVLVGTVQHRDGQTCDVTLENGLHVTGSAKALKGLRPERVELVIRPENIRL
GPVASMPWQATVIDSIYLGDHLRVHLRLGHQQALIVKVANNGFFKQLRTGQVTGFDWSTD
DAHLFELS
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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