SitesBLAST
Comparing AO353_12265 FitnessBrowser__pseudo3_N2E3:AO353_12265 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)
55% identity, 97% coverage: 6:271/274 of query aligns to 2:267/382 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
7aheC Opua inhibited inward facing (see paper)
55% identity, 97% coverage: 6:271/274 of query aligns to 2:267/382 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)
55% identity, 94% coverage: 6:263/274 of query aligns to 2:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F16), T39 (≠ V43), S61 (= S65), G62 (= G66), G64 (= G68), K65 (= K69), S66 (= S70), T67 (= T71), Q111 (= Q115), K161 (≠ H165), Q162 (= Q166), S164 (= S168), G166 (= G170), M167 (= M171), Q188 (≠ E192), H221 (= H225)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
40% identity, 83% coverage: 41:267/274 of query aligns to 17:243/375 of 2d62A
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
43% identity, 81% coverage: 49:269/274 of query aligns to 21:238/241 of 4u00A
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)
38% identity, 81% coverage: 46:267/274 of query aligns to 33:248/378 of P69874
- F45 (≠ I58) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S67) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ V73) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V89) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V154) mutation to M: Loss of ATPase activity and transport.
- D172 (= D191) 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)
38% identity, 83% coverage: 41:267/274 of query aligns to 14:240/372 of 1g291
- binding magnesium ion: D69 (≠ Q96), E71 (≠ D98), K72 (≠ M99), K79 (≠ R106), D80 (≠ R107)
- binding pyrophosphate 2-: S38 (= S65), G39 (= G66), C40 (≠ S67), G41 (= G68), K42 (= K69), T43 (≠ S70), T44 (= T71)
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)
38% identity, 84% coverage: 40:268/274 of query aligns to 15:242/343 of P30750
- 40:46 (vs. 65:71, 86% identical) binding
- E166 (= E192) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
37% identity, 84% coverage: 40:268/274 of query aligns to 16:243/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: I19 (≠ V43), S41 (= S65), G42 (= G66), A43 (≠ S67), G44 (= G68), K45 (= K69), S46 (= S70), T47 (= T71), N141 (≠ Q166), S143 (= S168), Q146 (≠ M171), H200 (= H225)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
37% identity, 84% coverage: 40:268/274 of query aligns to 16:243/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
37% identity, 84% coverage: 40:268/274 of query aligns to 16:243/344 of 3tuiC
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
38% identity, 81% coverage: 49:269/274 of query aligns to 20:238/240 of 4ymuJ
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)
37% identity, 83% coverage: 41:267/274 of query aligns to 13:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S65), G38 (= G66), C39 (≠ S67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), Q81 (= Q115), R128 (≠ K162), A132 (≠ Q166), S134 (= S168), G136 (= G170), Q137 (≠ M171), E158 (= E192), H191 (= H225)
- binding magnesium ion: S42 (= S70), Q81 (= Q115)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 83% coverage: 41:267/274 of query aligns to 13:233/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G66), C39 (≠ S67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), R128 (≠ K162), S134 (= S168), Q137 (≠ M171)
- binding beryllium trifluoride ion: S37 (= S65), G38 (= G66), K41 (= K69), Q81 (= Q115), S134 (= S168), G136 (= G170), H191 (= H225)
- binding magnesium ion: S42 (= S70), Q81 (= Q115)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 83% coverage: 41:267/274 of query aligns to 13:233/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ G45), G38 (= G66), C39 (≠ S67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), R128 (≠ K162), A132 (≠ Q166), S134 (= S168), Q137 (≠ M171)
- binding tetrafluoroaluminate ion: S37 (= S65), G38 (= G66), K41 (= K69), Q81 (= Q115), S134 (= S168), G135 (= G169), G136 (= G170), E158 (= E192), H191 (= H225)
- binding magnesium ion: S42 (= S70), Q81 (= Q115)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 83% coverage: 41:267/274 of query aligns to 13:233/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ G45), G38 (= G66), C39 (≠ S67), G40 (= G68), K41 (= K69), S42 (= S70), T43 (= T71), R128 (≠ K162), A132 (≠ Q166), S134 (= S168), Q137 (≠ M171)
- binding magnesium ion: S42 (= S70), Q81 (= Q115)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 83% coverage: 41:267/274 of query aligns to 13:233/374 of 2awnB
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)
37% identity, 83% coverage: 41:267/274 of query aligns to 14:234/371 of P68187
- A85 (≠ G118) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S139) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A147) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ W150) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ N152) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ Q157) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G170) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D191) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E261) 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)
37% identity, 83% coverage: 41:267/274 of query aligns to 11:231/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S65), G36 (= G66), C37 (≠ S67), G38 (= G68), K39 (= K69), S40 (= S70), T41 (= T71), R126 (≠ K162), A130 (≠ Q166), S132 (= S168), G134 (= G170), Q135 (≠ M171)
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)
34% identity, 96% coverage: 5:267/274 of query aligns to 2:234/369 of P19566
- L86 (= L119) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (≠ A193) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D198) 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.
Query Sequence
>AO353_12265 FitnessBrowser__pseudo3_N2E3:AO353_12265
MSNAAKIEVKNVFKIFGDRSADALDMIRQNKSKDQVLAETGCVIGVNDLSLSIATGEIFV
IMGLSGSGKSTLVRHINRLIDPTSGVILVDGVDILQYDMEALREFRRHKISMVFQSFGLL
PHKNVLDNVAYGLKVRGESKQVCAERAQHWINTVGLQGYENKYPHQLSGGMRQRVGLARA
LAADTDIILMDEAFSALDPLIRAEMQDQLLELQQTLHKTIVFITHDLDEAVRIGNRIAIL
KDGQLIQVGTPKEILHSPADEYVDRFVQRRAAVV
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