SitesBLAST
Comparing Ac3H11_2553 FitnessBrowser__acidovorax_3H11:Ac3H11_2553 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)
3c4jA Abc protein artp in complex with atp-gamma-s
62% identity, 92% coverage: 18:262/265 of query aligns to 3:242/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
62% identity, 92% coverage: 18:262/265 of query aligns to 3:242/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
62% identity, 92% coverage: 18:262/265 of query aligns to 3:242/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
62% identity, 92% coverage: 18:262/265 of query aligns to 3:242/242 of 2oljA
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
61% identity, 93% coverage: 17:262/265 of query aligns to 1:240/241 of 4u00A
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
58% identity, 92% coverage: 18:262/265 of query aligns to 1:240/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F28), V16 (= V33), S36 (= S53), G37 (= G54), S38 (= S55), G39 (= G56), K40 (= K57), S41 (= S58), T42 (= T59), E162 (= E184), H194 (= H216)
- binding magnesium ion: S41 (= S58), E162 (= E184)
1b0uA Atp-binding subunit of the histidine permease from salmonella typhimurium (see paper)
50% identity, 91% coverage: 24:264/265 of query aligns to 8:255/258 of 1b0uA
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)
49% identity, 94% coverage: 15:262/265 of query aligns to 3:257/258 of P02915
- S41 (= S53) binding
- G42 (= G54) binding
- G44 (= G56) binding
- K45 (= K57) binding
- S46 (= S58) binding
- T47 (= T59) binding
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 92% coverage: 18:262/265 of query aligns to 1:245/343 of P30750
- 40:46 (vs. 53:59, 86% identical) binding
- E166 (= E184) 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
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
39% identity, 92% coverage: 18:262/265 of query aligns to 2:246/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
39% identity, 92% coverage: 18:262/265 of query aligns to 2:246/344 of 3tuiC
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
39% identity, 92% coverage: 18:262/265 of query aligns to 2:246/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (= F28), Q14 (vs. gap), I19 (≠ V33), S41 (= S53), G42 (= G54), A43 (≠ S55), G44 (= G56), K45 (= K57), S46 (= S58), T47 (= T59), N141 (≠ S158), S143 (= S160), Q146 (= Q163), H200 (= H216)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
39% identity, 91% coverage: 19:258/265 of query aligns to 4:234/369 of P19566
- L86 (= L110) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P185) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D190) 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.
P0AAH0 Phosphate import ATP-binding protein PstB; ABC phosphate transporter; Phosphate-transporting ATPase; EC 7.3.2.1 from Escherichia coli (strain K12) (see paper)
36% identity, 93% coverage: 13:258/265 of query aligns to 5:252/257 of P0AAH0
- G48 (= G56) mutation to I: Loss of phosphate transport.
- K49 (= K57) mutation to Q: Loss of phosphate transport.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 91% coverage: 19:258/265 of query aligns to 4:234/371 of P68187
- A85 (≠ N109) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S131) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A139) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L142) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ T144) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A149) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G162) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D183) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E252) 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, 91% coverage: 19:258/265 of query aligns to 3:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F28), S37 (= S53), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), Q81 (= Q106), R128 (≠ A154), A132 (≠ S158), S134 (= S160), G136 (= G162), Q137 (= Q163), E158 (= E184), H191 (= H216)
- binding magnesium ion: S42 (= S58), Q81 (= Q106)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 91% coverage: 19:258/265 of query aligns to 3:233/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F28), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), R128 (≠ A154), S134 (= S160), Q137 (= Q163)
- binding beryllium trifluoride ion: S37 (= S53), G38 (= G54), K41 (= K57), Q81 (= Q106), S134 (= S160), G136 (= G162), H191 (= H216)
- binding magnesium ion: S42 (= S58), Q81 (= Q106)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 91% coverage: 19:258/265 of query aligns to 3:233/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F28), V17 (= V33), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), R128 (≠ A154), A132 (≠ S158), S134 (= S160), Q137 (= Q163)
- binding tetrafluoroaluminate ion: S37 (= S53), G38 (= G54), K41 (= K57), Q81 (= Q106), S134 (= S160), G135 (= G161), G136 (= G162), E158 (= E184), H191 (= H216)
- binding magnesium ion: S42 (= S58), Q81 (= Q106)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 91% coverage: 19:258/265 of query aligns to 3:233/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F28), V17 (= V33), G38 (= G54), C39 (≠ S55), G40 (= G56), K41 (= K57), S42 (= S58), T43 (= T59), R128 (≠ A154), A132 (≠ S158), S134 (= S160), Q137 (= Q163)
- binding magnesium ion: S42 (= S58), Q81 (= Q106)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 91% coverage: 19:258/265 of query aligns to 3:233/374 of 2awnB
Query Sequence
>Ac3H11_2553 FitnessBrowser__acidovorax_3H11:Ac3H11_2553
MKKEALPMNGAGQAAEPIVRIRGLRKAFGSHVVLNGIDFDVLPSQVVVVIGPSGSGKSTF
LRCCNGLEQPEGGSVEICGRTLVQDGRMLPDHDLNALREEVGMVFQSFNLFPHLSVLDNV
TLGPRKLRGLSRKEAEERAQALLTKVGLAHKAPAMPASLSGGQKQRVAIARALAMEPRVM
LFDEPTSALDPELVGEVLQVMKLLASEGMTMMVVTHEMDFAREVGDVVVVMDGGGIIEAG
APATIFTNPTQERTRSFLQAVLTRA
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