SitesBLAST
Comparing Pf1N1B4_1134 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1134 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)
42% identity, 61% coverage: 8:240/385 of query aligns to 30:263/382 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)
42% identity, 61% coverage: 8:240/385 of query aligns to 30:263/382 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)
41% identity, 60% coverage: 8:237/385 of query aligns to 30:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ D17), S61 (= S40), G62 (= G41), G64 (= G43), K65 (= K44), S66 (= S45), T67 (= T46), Q111 (= Q86), K161 (≠ R138), Q162 (≠ E139), S164 (= S141), G166 (= G143), M167 (≠ Q144), Q188 (≠ E165), H221 (= H198)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
40% identity, 62% coverage: 2:241/385 of query aligns to 7:244/375 of 2d62A
1g291 Malk (see paper)
39% identity, 62% coverage: 2:241/385 of query aligns to 4:241/372 of 1g291
- binding magnesium ion: D69 (= D71), E71 (≠ D73), K72 (≠ E74), K79 (vs. gap), D80 (≠ R78)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (≠ S45), T44 (= T46)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 62% coverage: 2:241/385 of query aligns to 3:234/374 of 2awnB
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, 62% coverage: 2:241/385 of query aligns to 3:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F11), S37 (= S40), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), Q81 (= Q86), R128 (= R135), A132 (≠ E139), S134 (= S141), G136 (= G143), Q137 (= Q144), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S45), Q81 (= Q86)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 62% coverage: 2:241/385 of query aligns to 3:234/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F11), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (= R135), S134 (= S141), Q137 (= Q144)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q86), S134 (= S141), G136 (= G143), H191 (= H198)
- binding magnesium ion: S42 (= S45), Q81 (= Q86)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 62% coverage: 2:241/385 of query aligns to 3:234/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (≠ K19), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (= R135), A132 (≠ E139), S134 (= S141), Q137 (= Q144)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q86), S134 (= S141), G135 (= G142), G136 (= G143), E158 (= E165), H191 (= H198)
- binding magnesium ion: S42 (= S45), Q81 (= Q86)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 62% coverage: 2:241/385 of query aligns to 3:234/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (≠ K19), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (= R135), A132 (≠ E139), S134 (= S141), Q137 (= Q144)
- binding magnesium ion: S42 (= S45), Q81 (= Q86)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 62% coverage: 2:241/385 of query aligns to 4:235/371 of P68187
- A85 (≠ G89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L121) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ S123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K130) 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.
- R228 (≠ D234) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 62% coverage: 2:241/385 of query aligns to 1:232/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F11), S35 (= S40), G36 (= G41), C37 (= C42), G38 (= G43), K39 (= K44), S40 (= S45), T41 (= T46), R126 (= R135), A130 (≠ E139), S132 (= S141), G134 (= G143), Q135 (= Q144)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
40% identity, 62% coverage: 2:241/385 of query aligns to 7:230/353 of 1vciA
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
35% identity, 62% coverage: 2:241/385 of query aligns to 4:235/369 of P19566
- L86 (= L90) 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.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
36% identity, 63% coverage: 1:242/385 of query aligns to 17:250/378 of P69874
- C26 (≠ T10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ I33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I125) 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:
- 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
36% identity, 63% coverage: 1:242/385 of query aligns to 2:235/358 of 8y5iA
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 64% coverage: 1:247/385 of query aligns to 1:235/348 of 3d31A
Sites not aligning to the query:
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
33% identity, 62% coverage: 1:240/385 of query aligns to 1:241/343 of P30750
- 40:46 (vs. 40:46, 86% identical) binding ATP
- E166 (= E165) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding L-methionine
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding L-methionine
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 58% coverage: 20:241/385 of query aligns to 16:233/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
37% identity, 62% coverage: 2:241/385 of query aligns to 3:235/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F11), S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (= S45), Q82 (= Q86), Q133 (≠ E139), G136 (= G142), G137 (= G143), Q138 (= Q144), H192 (= H198)
- binding magnesium ion: S43 (= S45), Q82 (= Q86)
Query Sequence
>Pf1N1B4_1134 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1134
MIELQNLSKTFQSNGKDVKAVDSVSLTVNEGEICVFLGPSGCGKSTTLKMINRLIKPTSG
KILINGEDTTDLDEVTLRRNIGYVIQQIGLFPNMTIEENITIVPRLLGWDKQKCHDRARE
LMSMIKLEPKQYLNRYPRELSGGQQQRIGVIRALAADAPLLLMDEPFGAVDPINREMIQN
EFFEMQRALNKTVIMVSHDIDEAIKLGDKIAIFRAGKLLQIDHPDTLLAHPADDFVSNFV
GQDSTLKRLLLVKAEDAADNAPSVSPETPVAEALELMDELDRRYVVVTCAENKALGYVRR
RDLHRQTGTCAQYLREFNATAAYDEHLRILLSRMYEFNRSWLPVMDAERVFLGEVTQESI
AEYLSSGKSRGGKTSIVSPAEAAVA
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