SitesBLAST
Comparing AO356_09255 FitnessBrowser__pseudo5_N2C3_1:AO356_09255 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)
52% identity, 76% coverage: 11:291/372 of query aligns to 1:273/382 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)
52% identity, 76% coverage: 11:291/372 of query aligns to 1:273/382 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)
53% identity, 70% coverage: 11:270/372 of query aligns to 1:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F22), T39 (≠ V50), S61 (= S72), G62 (= G73), G64 (= G75), K65 (= K76), S66 (= S77), T67 (= T78), Q111 (= Q122), K161 (≠ S172), Q162 (≠ E173), S164 (= S175), G166 (= G177), M167 (= M178), Q188 (≠ E199), H221 (= H232)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 61% coverage: 53:278/372 of query aligns to 33:252/378 of P69874
- F45 (≠ I65) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S74) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I80) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V96) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V161) mutation to M: Loss of ATPase activity and transport.
- D172 (= D198) 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)
37% identity, 70% coverage: 17:275/372 of query aligns to 8:241/372 of 1g291
- binding magnesium ion: D69 (≠ T103), E71 (≠ S105), K72 (≠ A106), K79 (≠ R113), D80 (≠ A114)
- binding pyrophosphate 2-: S38 (= S72), G39 (= G73), C40 (≠ S74), G41 (= G75), K42 (= K76), T43 (≠ S77), T44 (= T78)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 63% coverage: 43:275/372 of query aligns to 12:244/375 of 2d62A
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 72% coverage: 33:300/372 of query aligns to 10:267/343 of P30750
- 40:46 (vs. 72:78, 86% identical) binding
- E166 (= E199) 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)
38% identity, 72% coverage: 33:300/372 of query aligns to 11:268/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (≠ V34), Q14 (= Q36), I19 (≠ L44), S41 (= S72), G42 (= G73), A43 (≠ S74), G44 (= G75), K45 (= K76), S46 (= S77), T47 (= T78), N141 (≠ E173), S143 (= S175), Q146 (≠ M178), H200 (= H232)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
38% identity, 72% coverage: 33:300/372 of query aligns to 11:268/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
38% identity, 72% coverage: 33:300/372 of query aligns to 11:268/344 of 3tuiC
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
39% identity, 63% coverage: 43:277/372 of query aligns to 7:239/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ Y47), V16 (≠ G52), S36 (= S72), G37 (= G73), S38 (= S74), G39 (= G75), K40 (= K76), S41 (= S77), T42 (= T78), E162 (= E199), H194 (= H232)
- binding magnesium ion: S41 (= S77), E162 (= E199)
7d0aB Acinetobacter mlafedb complex in adp-vanadate trapped vclose conformation (see paper)
41% identity, 60% coverage: 55:276/372 of query aligns to 22:242/263 of 7d0aB
7d08B Acinetobacter mlafedb complex in atp-bound vtrans1 conformation (see paper)
41% identity, 60% coverage: 55:276/372 of query aligns to 22:242/263 of 7d08B
Sites not aligning to the query:
6z5uK Cryo-em structure of the a. Baumannii mlabdef complex bound to appnhp (see paper)
41% identity, 60% coverage: 55:276/372 of query aligns to 20:240/253 of 6z5uK
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
44% identity, 60% coverage: 53:275/372 of query aligns to 19:239/350 of 3fvqB
- binding adenosine-5'-triphosphate: S38 (= S72), G39 (= G73), C40 (≠ S74), G41 (= G75), K42 (= K76), T43 (≠ S77), T44 (= T78), R133 (= R169), E137 (= E173), S139 (= S175), G141 (= G177), Q142 (≠ M178)
- binding calcium ion: T43 (≠ S77), Q86 (= Q122)
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)
39% identity, 60% coverage: 53:274/372 of query aligns to 20:235/393 of P9WQI3
- H193 (= H232) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 66% coverage: 30:275/372 of query aligns to 1:235/371 of P68187
- A85 (= A125) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G146) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A154) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A157) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A159) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ S164) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G177) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D198) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D268) 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
36% identity, 62% coverage: 47:275/372 of query aligns to 13:235/369 of P19566
- L86 (= L126) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P200) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D205) 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)
37% identity, 62% coverage: 47:275/372 of query aligns to 10:232/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y47), S35 (= S72), G36 (= G73), C37 (≠ S74), G38 (= G75), K39 (= K76), S40 (= S77), T41 (= T78), R126 (= R169), A130 (≠ E173), S132 (= S175), G134 (= G177), Q135 (≠ M178)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 62% coverage: 47:275/372 of query aligns to 12:234/374 of 2awnB
Query Sequence
>AO356_09255 FitnessBrowser__pseudo5_N2C3_1:AO356_09255
MTTAKIDTNEVLVDCQNVWKIFGESAPAAMQAVVQQGLTKTRILQDYSCVVGVSNVSLQV
RRGEIFCIMGLSGSGKSTLIRLLNKLITPSSGKVLVKGKDLSTLSAAQLREVRARHIGMV
FQSVALLPNRTVLENTAFGLEVQGIGKAERYKVAERALAKVGLSEWSQRYPSELSGGMQQ
RVGLARAITADPEVILMDEPFSALDPLIRRQLQDEFRQLTKELGKSAVFITHDLDEAIRI
GDRIAIMKDGVIIQVGTAEEIVLKPADDYVAEFVAGISRLHLVKAHSVMTPVAPFKAANP
GCDIARLIKTRLDADINELIGLTVKSERDALAVVDNDVVVGIITPRDLLRGVQGIANEFS
ASSATAALEASA
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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