SitesBLAST
Comparing AO356_10410 FitnessBrowser__pseudo5_N2C3_1:AO356_10410 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)
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
54% identity, 89% coverage: 12:242/260 of query aligns to 9:239/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F14), V16 (= V19), S36 (= S39), G37 (= G40), S38 (≠ C41), G39 (= G42), K40 (= K43), S41 (= S44), T42 (= T45), E162 (= E165), H194 (= H197)
- binding magnesium ion: S41 (= S44), E162 (= E165)
3c4jA Abc protein artp in complex with atp-gamma-s
54% identity, 92% coverage: 4:241/260 of query aligns to 3:240/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
54% identity, 92% coverage: 4:241/260 of query aligns to 3:240/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
54% identity, 92% coverage: 4:241/260 of query aligns to 3:240/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
54% identity, 92% coverage: 4:241/260 of query aligns to 3:240/242 of 2oljA
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
52% identity, 93% coverage: 4:244/260 of query aligns to 2:241/241 of 4u00A
P02915 Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP; EC 7.4.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
44% identity, 89% coverage: 10:240/260 of query aligns to 12:254/258 of P02915
- S41 (= S39) binding
- G42 (= G40) binding
- G44 (= G42) binding
- K45 (= K43) binding
- S46 (= S44) binding
- T47 (= T45) binding
1b0uA Atp-binding subunit of the histidine permease from salmonella typhimurium (see paper)
44% identity, 89% coverage: 10:240/260 of query aligns to 8:250/258 of 1b0uA
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 92% coverage: 4:241/260 of query aligns to 1:243/343 of P30750
- 40:46 (vs. 39:45, 86% identical) binding
- E166 (= E165) 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, 92% coverage: 4:241/260 of query aligns to 2:244/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (= F14), Q14 (≠ E16), I19 (vs. gap), S41 (= S39), G42 (= G40), A43 (≠ C41), G44 (= G42), K45 (= K43), S46 (= S44), T47 (= T45), N141 (≠ Q139), S143 (= S141), Q146 (= Q144), H200 (= H197)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
37% identity, 92% coverage: 4:241/260 of query aligns to 2:244/344 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, 92% coverage: 4:241/260 of query aligns to 2:244/344 of 3tuiC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 89% coverage: 1:232/260 of query aligns to 14:241/378 of P69874
- C26 (≠ F13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F14) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V32) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C41) mutation to T: Loss of ATPase activity and transport.
- L60 (= L47) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F63) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V127) 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.
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
36% identity, 90% coverage: 24:258/260 of query aligns to 46:282/382 of 7ahhC
- 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: L275 (≠ T251)
- binding phosphoaminophosphonic acid-adenylate ester: G62 (= G40), G64 (= G42), K65 (= K43), D187 (= D164), E188 (= E165)
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: 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
36% identity, 90% coverage: 24:258/260 of query aligns to 46:282/382 of 7aheC
- 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: L275 (≠ T251)
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: 297, 298
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 92% coverage: 3:242/260 of query aligns to 1:232/374 of 2awnB
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
39% identity, 87% coverage: 1:225/260 of query aligns to 1:228/648 of P75831
- K47 (= K43) mutation to L: Lack of activity.
- D169 (= D164) mutation to N: Lack of activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 92% coverage: 3:242/260 of query aligns to 2:233/371 of P68187
- A85 (≠ H90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K110) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A122) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V127) 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 (≠ Q237) 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.
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, 92% coverage: 3:242/260 of query aligns to 1:232/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F14), S37 (= S39), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), Q81 (= Q87), R128 (≠ K132), A132 (≠ Q139), S134 (= S141), G136 (= G143), Q137 (= Q144), E158 (= E165), H191 (= H197)
- binding magnesium ion: S42 (= S44), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 92% coverage: 3:242/260 of query aligns to 1:232/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F14), G38 (= G40), C39 (= C41), G40 (= G42), K41 (= K43), S42 (= S44), T43 (= T45), R128 (≠ K132), S134 (= S141), Q137 (= Q144)
- binding beryllium trifluoride ion: S37 (= S39), G38 (= G40), K41 (= K43), Q81 (= Q87), S134 (= S141), G136 (= G143), H191 (= H197)
- binding magnesium ion: S42 (= S44), Q81 (= Q87)
Query Sequence
>AO356_10410 FitnessBrowser__pseudo5_N2C3_1:AO356_10410
MSALIEFKGFNKFFGEQQVLDGIDLQVQSGEVIVILGPSGCGKSTLLRCLNGLEVAHSGS
LAFAGRELLDKGTDWREVRQQIGMVFQSYHLFPHMSVLDNLLLGPVKVQKRDRREARAQA
EALLARVGLLDKRDAFPRQLSGGQQQRIAIVRSLCMNPKVMLFDEVTAALDPEMVKEVLE
VIQGLAREGMTLLIVTHEMAFARAVADRIVFMDAGRILEQNPPEIFFTNPQTARAQQFLE
KFSYVAALPKTTQTKELELS
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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