SitesBLAST
Comparing GFF2277 FitnessBrowser__WCS417:GFF2277 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)
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 95% coverage: 12:251/252 of query aligns to 4:253/254 of 1g6hA
1g9xB Characterization of the twinning structure of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 95% coverage: 12:251/252 of query aligns to 4:253/253 of 1g9xB
1ji0A Crystal structure analysis of the abc transporter from thermotoga maritima
34% identity, 95% coverage: 12:251/252 of query aligns to 6:238/240 of 1ji0A
5x40A Structure of a cbio dimer bound with amppcp (see paper)
32% identity, 92% coverage: 11:242/252 of query aligns to 3:230/280 of 5x40A
- binding phosphomethylphosphonic acid adenylate ester: F14 (= F22), V18 (≠ F25), A20 (= A27), N40 (= N47), G41 (= G48), G43 (= G50), K44 (= K51), S45 (≠ T52), T46 (= T53), Q88 (≠ K92), H139 (≠ D152), M140 (≠ L153), L141 (= L154), S142 (= S155), G144 (= G157), Q145 (= Q158), Q166 (≠ E179), H198 (= H210)
- binding magnesium ion: S45 (≠ T52), Q88 (≠ K92)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
29% identity, 93% coverage: 11:244/252 of query aligns to 16:240/378 of P69874
- C26 (≠ S21) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F22) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ A49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I141) mutation to M: Loss of ATPase activity and transport.
- D172 (= D178) 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.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
31% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of 1oxuA
Sites not aligning to the query:
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
31% identity, 88% coverage: 27:248/252 of query aligns to 20:237/353 of Q97UY8
- S142 (= S155) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G157) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E179) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 88% coverage: 25:245/252 of query aligns to 18:234/343 of P30750
- 40:46 (vs. 47:53, 71% identical) binding
- E166 (= E179) 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
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 85% coverage: 30:243/252 of query aligns to 21:225/369 of P19566
- L86 (≠ I98) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P180) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ S185) 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.
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
30% identity, 88% coverage: 25:245/252 of query aligns to 19:235/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: I19 (≠ F25), S41 (≠ N47), G42 (= G48), A43 (= A49), G44 (= G50), K45 (= K51), S46 (≠ T52), T47 (= T53), N141 (≠ L153), S143 (= S155), Q146 (= Q158), H200 (= H210)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
30% identity, 88% coverage: 25:245/252 of query aligns to 19:235/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
30% identity, 88% coverage: 25:245/252 of query aligns to 19:235/344 of 3tuiC
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)
33% identity, 85% coverage: 30:243/252 of query aligns to 21:225/371 of P68187
- A85 (≠ S97) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V134) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V137) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R139) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G144) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G157) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D178) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
33% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (≠ N47), G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), Q81 (= Q94), R128 (≠ Q149), A132 (≠ L153), S134 (= S155), G136 (= G157), Q137 (= Q158), E158 (= E179), H191 (= H210)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
33% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ Q149), S134 (= S155), Q137 (= Q158)
- binding beryllium trifluoride ion: S37 (≠ N47), G38 (= G48), K41 (= K51), Q81 (= Q94), S134 (= S155), G136 (= G157), H191 (= H210)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
33% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ Q149), A132 (≠ L153), S134 (= S155), Q137 (= Q158)
- binding tetrafluoroaluminate ion: S37 (≠ N47), G38 (= G48), K41 (= K51), Q81 (= Q94), S134 (= S155), G135 (≠ H156), G136 (= G157), E158 (= E179), H191 (= H210)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
33% identity, 85% coverage: 30:243/252 of query aligns to 20:224/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G48), C39 (≠ A49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ Q149), A132 (≠ L153), S134 (= S155), Q137 (= Q158)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q94)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
34% identity, 81% coverage: 30:234/252 of query aligns to 20:215/374 of 2awnB
Sites not aligning to the query:
Query Sequence
>GFF2277 FitnessBrowser__WCS417:GFF2277
MTAVGFEMKKPVLAIEGLTVSFDGFKAVDNLNLYIDRNEVRVVIGPNGAGKTTVLDLICG
KTRATSGSIQFDGQELTNMREYNIVRAGVGRKFQNPSIYENLTVFENLEMSYPAGRKVWG
ALFFKRNAQVIARVEEVAREIFLGDLLQQQADLLSHGQKQWLEIGMLLMQDPELLMLDEP
VAGMSVNERAQTAELLNRISQGRSVLVIEHDMEFVKSIAHKVTVLHQGKVLAEGSMASVQ
SNPKVIEVYLGH
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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