SitesBLAST
Comparing Pf1N1B4_1583 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1583 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)
56% identity, 96% coverage: 8:273/276 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)
56% identity, 96% coverage: 8:273/276 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)
56% identity, 93% coverage: 8:265/276 of query aligns to 2:259/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F18), T39 (≠ V45), S61 (= S67), G62 (= G68), G64 (= G70), K65 (= K71), S66 (= S72), T67 (= T73), Q111 (= Q117), K161 (≠ H167), Q162 (= Q168), S164 (= S170), G166 (= G172), M167 (= M173), Q188 (≠ E194), H221 (= H227)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
40% identity, 82% coverage: 43:269/276 of query aligns to 17:243/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 80% coverage: 48:269/276 of query aligns to 33:248/378 of P69874
- F45 (≠ I60) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S69) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ V75) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V91) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V156) mutation to M: Loss of ATPase activity and transport.
- D172 (= D193) 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
39% identity, 80% coverage: 48:269/276 of query aligns to 18:233/358 of 8y5iA
Sites not aligning to the query:
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
42% identity, 80% coverage: 51:271/276 of query aligns to 21:238/241 of 4u00A
Sites not aligning to the query:
1g291 Malk (see paper)
38% identity, 82% coverage: 43:269/276 of query aligns to 14:240/372 of 1g291
- binding magnesium ion: D69 (≠ Q98), E71 (≠ D100), K72 (≠ M101), K79 (≠ R108), D80 (≠ R109)
- binding pyrophosphate 2-: S38 (= S67), G39 (= G68), C40 (≠ S69), G41 (= G70), K42 (= K71), T43 (≠ S72), T44 (= T73)
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, 83% coverage: 42:270/276 of query aligns to 15:242/343 of P30750
- 40:46 (vs. 67:73, 86% identical) binding ATP
- E166 (= E194) 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
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
38% identity, 83% coverage: 42:270/276 of query aligns to 16:243/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: I19 (≠ V45), S41 (= S67), G42 (= G68), A43 (≠ S69), G44 (= G70), K45 (= K71), S46 (= S72), T47 (= T73), N141 (≠ Q168), S143 (= S170), Q146 (≠ M173), H200 (= H227)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
38% identity, 83% coverage: 42:270/276 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)
38% identity, 83% coverage: 42:270/276 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, 80% coverage: 51:271/276 of query aligns to 20:238/240 of 4ymuJ
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, 82% coverage: 43:269/276 of query aligns to 13:233/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 82% coverage: 43:269/276 of query aligns to 11:231/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S67), G36 (= G68), C37 (≠ S69), G38 (= G70), K39 (= K71), S40 (= S72), T41 (= T73), R126 (≠ K164), A130 (≠ Q168), S132 (= S170), G134 (= G172), Q135 (≠ M173)
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, 82% coverage: 43:269/276 of query aligns to 13:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S67), G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), Q81 (= Q117), R128 (≠ K164), A132 (≠ Q168), S134 (= S170), G136 (= G172), Q137 (≠ M173), E158 (= E194), H191 (= H227)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
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, 82% coverage: 43:269/276 of query aligns to 13:233/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (≠ K164), S134 (= S170), Q137 (≠ M173)
- binding beryllium trifluoride ion: S37 (= S67), G38 (= G68), K41 (= K71), Q81 (= Q117), S134 (= S170), G136 (= G172), H191 (= H227)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
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, 82% coverage: 43:269/276 of query aligns to 13:233/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ G47), G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (≠ K164), A132 (≠ Q168), S134 (= S170), Q137 (≠ M173)
- binding tetrafluoroaluminate ion: S37 (= S67), G38 (= G68), K41 (= K71), Q81 (= Q117), S134 (= S170), G135 (= G171), G136 (= G172), E158 (= E194), H191 (= H227)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 82% coverage: 43:269/276 of query aligns to 13:233/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ G47), G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (≠ K164), A132 (≠ Q168), S134 (= S170), Q137 (≠ M173)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
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, 82% coverage: 43:269/276 of query aligns to 14:234/371 of P68187
- A85 (≠ G120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S141) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A149) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ W152) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ N154) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K159) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G172) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D193) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E263) 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.
Query Sequence
>Pf1N1B4_1583 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1583
MSNEAISKIEVKNVFKIFGNRSKDALEMIRQKKTKDQVLAETGCVVGVNDLSLSIGTGEI
FVIMGLSGSGKSTLVRHFNRLIDPTSGAILVDGVDILQYDMEALREFRRHKISMVFQSFG
LLPHKTVLDNVAYGLKVRGESKQMCAERALHWINTVGLKGYENKYPHQLSGGMRQRVGLA
RALAADTDIILMDEAFSALDPLIRAEMQDQLLELQKTLHKTIVFITHDLDEAVRIGNRIA
ILKDGRLIQVGTPREILHSPADEYVDRFVQRRAAVV
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