SitesBLAST
Comparing GFF2770 FitnessBrowser__Phaeo:GFF2770 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)
P04983 Ribose import ATP-binding protein RbsA; EC 7.5.2.7 from Escherichia coli (strain K12) (see paper)
37% identity, 94% coverage: 3:477/505 of query aligns to 2:474/501 of P04983
- K43 (= K44) mutation to R: Loss of transport.
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 56% coverage: 5:288/505 of query aligns to 1:307/343 of P30750
- 40:46 (vs. 40:46, 86% identical) binding
- E166 (= E163) mutation to Q: Exhibits little ATPase activity.
- VDAPLL 278:283 (≠ VPAPSA 260:265) binding
- N295 (≠ T276) mutation to A: Reduces the binding of L-methionine to undetectable levels.
- NI 295:296 (≠ TV 276:277) binding
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
29% identity, 56% coverage: 5:288/505 of query aligns to 2:308/344 of 3tuzC
- binding adenosine-5'-diphosphate: F12 (≠ Y15), Q14 (vs. gap), G42 (= G41), G44 (= G43), K45 (= K44), S46 (= S45), T47 (= T46)
- binding selenomethionine: F274 (≠ I255), V279 (= V260), A281 (= A262), P282 (= P263), L283 (≠ S264), L284 (≠ A265)
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
29% identity, 56% coverage: 5:288/505 of query aligns to 2:308/344 of 3tuiC
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
29% identity, 56% coverage: 5:288/505 of query aligns to 2:308/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (≠ Y15), Q14 (vs. gap), I19 (≠ V18), S41 (≠ N40), G42 (= G41), A43 (= A42), G44 (= G43), K45 (= K44), S46 (= S45), T47 (= T46), N141 (≠ D137), S143 (= S139), Q146 (≠ E142), H200 (= H195)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
34% identity, 41% coverage: 6:214/505 of query aligns to 3:210/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
34% identity, 41% coverage: 6:214/505 of query aligns to 3:210/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y15), S37 (≠ N40), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), Q81 (= Q87), R128 (= R133), A132 (≠ D137), S134 (= S139), G136 (= G141), Q137 (≠ E142), E158 (= E163), H191 (= H195)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
34% identity, 41% coverage: 6:214/505 of query aligns to 3:210/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (= R133), S134 (= S139), Q137 (≠ E142)
- binding beryllium trifluoride ion: S37 (≠ N40), G38 (= G41), K41 (= K44), Q81 (= Q87), S134 (= S139), G136 (= G141), H191 (= H195)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
34% identity, 41% coverage: 6:214/505 of query aligns to 3:210/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A20), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (= R133), A132 (≠ D137), S134 (= S139), Q137 (≠ E142)
- binding tetrafluoroaluminate ion: S37 (≠ N40), G38 (= G41), K41 (= K44), Q81 (= Q87), S134 (= S139), G135 (≠ A140), G136 (= G141), E158 (= E163), H191 (= H195)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
34% identity, 41% coverage: 6:214/505 of query aligns to 3:210/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A20), G38 (= G41), C39 (≠ A42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (= T46), R128 (= R133), A132 (≠ D137), S134 (= S139), Q137 (≠ E142)
- binding magnesium ion: S42 (= S45), Q81 (= Q87)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 41% coverage: 6:214/505 of query aligns to 4:211/371 of P68187
- A85 (≠ S90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ L111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V121) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ P128) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G141) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D162) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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)
34% identity, 41% coverage: 6:214/505 of query aligns to 1:208/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y15), S35 (≠ N40), G36 (= G41), C37 (≠ A42), G38 (= G43), K39 (= K44), S40 (= S45), T41 (= T46), R126 (= R133), A130 (≠ D137), S132 (= S139), G134 (= G141), Q135 (≠ E142)
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, 41% coverage: 6:214/505 of query aligns to 4:211/369 of P19566
- L86 (= L91) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P164) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ T169) 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.
3d31A Modbc from methanosarcina acetivorans (see paper)
32% identity, 43% coverage: 5:223/505 of query aligns to 1:214/348 of 3d31A
Sites not aligning to the query:
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
29% identity, 43% coverage: 2:218/505 of query aligns to 1:231/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
29% identity, 43% coverage: 2:218/505 of query aligns to 1:231/253 of 1g9xB
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
33% identity, 39% coverage: 1:198/505 of query aligns to 1:207/233 of P75957
- G42 (= G38) mutation to D: Loss of lipoprotein release when overexpressed.
7arlD Lolcde in complex with lipoprotein and adp (see paper)
33% identity, 38% coverage: 5:198/505 of query aligns to 2:204/222 of 7arlD
7mdyC Lolcde nucleotide-bound
33% identity, 38% coverage: 5:198/505 of query aligns to 2:204/226 of 7mdyC
- binding adp orthovanadate: Y12 (= Y15), G42 (= G41), S43 (≠ A42), G44 (= G43), K45 (= K44), S46 (= S45), T47 (= T46), Q91 (= Q87), H138 (≠ R133), E142 (≠ D137), S144 (= S139), G145 (≠ A140), G146 (= G141), E168 (= E163), N172 (≠ V167), H201 (= H195)
- binding magnesium ion: S46 (= S45), Q91 (= Q87)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 44% coverage: 4:223/505 of query aligns to 16:234/378 of P69874
- C26 (≠ A14) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y15) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A42) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ V48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ Y125) mutation to M: Loss of ATPase activity and transport.
- D172 (= D162) 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.
Query Sequence
>GFF2770 FitnessBrowser__Phaeo:GFF2770
MTQPLLSLQGLTKAYPGVVANDTVSFDIGAGEVHALLGENGAGKSTLVKMIYGLVKPDSG
KMLLHGEPYTPGEPRQARADGIAMVFQHFSLFDALNVAENIALGMETPPALRDLATQIRK
VSETYGLPLDPYRTVGDLSAGERQRVEIIRCLLQDPKLLIMDEPTSVLTPQEVEILFQTL
QKLRSEGTSILYISHKLEEIRTLCDHATILRLGKNVGECVPSETSARDMAEMMVGTALQT
PERSGRALGDVALDISGLSVPAPSAFGTALKNVHMTVRKGEILGVGGVAGNGQDELLGVL
SGETTTAADAVTLDGAPIGNLGPVARRRLGILAAPEERLGHAAAPDMSLTENAMLTAATR
EGLASRGFLKWGLAQEFAEKVIKSFDVRTPGPENAARSLSGGNLQKFVIGREVLQRPDVL
VVNQPTWGVDAAAAAAIRQSLLDLAAGGTAVICISQDLDELMEIADSFAALNEGRLSAPR
PTAGLSVDEIGLMMGGAHGMEVAHV
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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