SitesBLAST
Comparing Pf6N2E2_4681 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4681 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
54% identity, 68% coverage: 4:271/392 of query aligns to 3:266/382 of 7ahhC
- binding phosphoaminophosphonic acid-adenylate ester: F12 (= F13), K29 (≠ R30), T39 (≠ I40), V40 (= V41), G41 (= G42), S61 (= S62), G62 (= G63), S63 (= S64), G64 (= G65), K65 (= K66), S66 (= S67), T67 (≠ S68), D187 (= D192), E188 (= E193)
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: 272, 273, 275, 295, 296, 297, 298, 357, 370, 372
7aheC Opua inhibited inward facing (see paper)
54% identity, 68% coverage: 4:271/392 of query aligns to 3:266/382 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, 295, 296, 297, 298, 357, 372
7ahdC Opua (e190q) occluded (see paper)
54% identity, 67% coverage: 4:265/392 of query aligns to 3:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F13), K29 (≠ R30), T39 (≠ I40), S61 (= S62), G62 (= G63), S63 (= S64), G64 (= G65), K65 (= K66), S66 (= S67), T67 (≠ S68), Q111 (= Q116), K161 (≠ D166), Q162 (≠ E167), S164 (= S169), G166 (= G171), M167 (= M172), Q188 (≠ E193), H221 (= H226)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 59% coverage: 43:275/392 of query aligns to 33:255/378 of P69874
- F45 (≠ I55) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S64) mutation to T: Loss of ATPase activity and transport.
- L60 (= L70) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V86) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V155) mutation to M: Loss of ATPase activity and transport.
- D172 (= D192) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
40% identity, 63% coverage: 33:277/392 of query aligns to 12:251/375 of 2d62A
1g291 Malk (see paper)
40% identity, 61% coverage: 38:277/392 of query aligns to 14:248/372 of 1g291
- binding magnesium ion: D69 (≠ S97), E71 (≠ S99), K72 (≠ P100), K79 (≠ R107), D80 (≠ T108), Y228 (≠ V256), D229 (≠ L257)
- binding pyrophosphate 2-: P37 (≠ L61), S38 (= S62), G39 (= G63), C40 (≠ S64), G41 (= G65), K42 (= K66), T43 (≠ S67), T44 (≠ S68)
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, 59% coverage: 38:268/392 of query aligns to 13:233/374 of 2awnB
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)
39% identity, 59% coverage: 38:268/392 of query aligns to 14:234/369 of P19566
- L86 (= L120) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P194) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D199) 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)
38% identity, 59% coverage: 38:268/392 of query aligns to 11:231/367 of 1q12A
- binding adenosine-5'-triphosphate: V15 (≠ G42), S35 (= S62), G36 (= G63), C37 (≠ S64), G38 (= G65), K39 (= K66), S40 (= S67), T41 (≠ S68), R126 (≠ K163), K129 (≠ D166), A130 (≠ E167), L131 (= L168), S132 (= S169), G133 (= G170), G134 (= G171), Q135 (≠ M172), N160 (≠ A197), H189 (= H226)
Sites not aligning to the query:
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
38% identity, 59% coverage: 38:268/392 of query aligns to 13:233/372 of 2awoA
Sites not aligning to the query:
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, 59% coverage: 38:268/392 of query aligns to 13:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: V17 (≠ G42), P36 (≠ L61), S37 (= S62), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), Q81 (= Q116), R128 (≠ K163), A132 (≠ E167), S134 (= S169), G135 (= G170), G136 (= G171), Q137 (≠ M172), E158 (= E193), H191 (= H226)
- binding magnesium ion: S42 (= S67), Q81 (= Q116), D157 (= D192)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 59% coverage: 38:268/392 of query aligns to 13:233/371 of 3puxA
- binding adenosine-5'-diphosphate: V17 (≠ G42), S37 (= S62), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), R128 (≠ K163), A132 (≠ E167), L133 (= L168), S134 (= S169), Q137 (≠ M172)
- binding beryllium trifluoride ion: S37 (= S62), G38 (= G63), K41 (= K66), Q81 (= Q116), S134 (= S169), G135 (= G170), G136 (= G171), E158 (= E193), H191 (= H226)
- binding magnesium ion: S42 (= S67), Q81 (= Q116), D157 (= D192)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 59% coverage: 38:268/392 of query aligns to 13:233/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ G42), S37 (= S62), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), R128 (≠ K163), A132 (≠ E167), S134 (= S169), Q137 (≠ M172)
- binding tetrafluoroaluminate ion: S37 (= S62), G38 (= G63), K41 (= K66), Q81 (= Q116), S134 (= S169), G135 (= G170), G136 (= G171), E158 (= E193), N162 (≠ A197), H191 (= H226)
- binding magnesium ion: S42 (= S67), Q81 (= Q116)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 59% coverage: 38:268/392 of query aligns to 14:234/371 of P68187
- A85 (= A119) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P140) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V148) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ K151) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E153) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T158) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G171) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D192) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D262) 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.
8hplC ABC transporter, ATP-binding protein SugC (see paper)
37% identity, 58% coverage: 42:268/392 of query aligns to 16:232/384 of 8hplC
Sites not aligning to the query:
8hprC ABC transporter, ATP-binding protein SugC (see paper)
32% identity, 83% coverage: 42:367/392 of query aligns to 18:342/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S62), G39 (= G63), C40 (≠ S64), G41 (= G65), K42 (= K66), S43 (= S67), T44 (≠ S68), Q82 (= Q116), G132 (≠ D166), Q133 (≠ E167), L134 (= L168), S135 (= S169), G136 (= G170), G137 (= G171), Q138 (≠ M172), H192 (= H226)
- binding magnesium ion: S43 (= S67), Q82 (= Q116)
Sites not aligning to the query:
8hprD ABC transporter, ATP-binding protein SugC (see paper)
37% identity, 58% coverage: 42:268/392 of query aligns to 18:234/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S62), C40 (≠ S64), G41 (= G65), K42 (= K66), S43 (= S67), T44 (≠ S68), Q82 (= Q116), R129 (≠ K163), G132 (≠ D166), Q133 (≠ E167), S135 (= S169), G136 (= G170), G137 (= G171), Q138 (≠ M172), Q159 (≠ E193), H192 (= H226)
- binding magnesium ion: S43 (= S67), Q82 (= Q116), D158 (= D192)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
37% identity, 63% coverage: 35:279/392 of query aligns to 14:242/353 of 1vciA