SitesBLAST
Comparing SM_b20485 FitnessBrowser__Smeli:SM_b20485 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)
39% identity, 96% coverage: 19:506/509 of query aligns to 4:490/501 of P04983
- K43 (= K58) mutation to R: Loss of transport.
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
32% identity, 43% coverage: 18:236/509 of query aligns to 1:215/241 of 4u00A
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
33% identity, 42% coverage: 20:235/509 of query aligns to 7:221/375 of 2d62A
1g291 Malk (see paper)
33% identity, 42% coverage: 20:235/509 of query aligns to 4:218/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (≠ H86), K72 (≠ M87), K79 (≠ Q93), D80 (= D94)
- binding pyrophosphate 2-: S38 (≠ N54), G39 (= G55), C40 (= C56), G41 (= G57), K42 (= K58), T43 (≠ S59), T44 (= T60)
Sites not aligning to the query:
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: 14:235/509 of query aligns to 12:226/378 of P69874
- C26 (≠ T28) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F29) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V47) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C56) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I62) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ Y79) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L145) mutation to M: Loss of ATPase activity and transport.
- D172 (= D182) 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
31% identity, 44% coverage: 20:241/509 of query aligns to 4:226/369 of P19566
- L86 (= L106) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P184) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (≠ T189) 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.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
29% identity, 43% coverage: 19:236/509 of query aligns to 1:215/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F29), V16 (≠ A34), S36 (≠ N54), G37 (= G55), S38 (≠ C56), G39 (= G57), K40 (= K58), S41 (= S59), T42 (= T60), E162 (= E183), H194 (= H215)
- binding magnesium ion: S41 (= S59), E162 (= E183)
P0A9R7 Cell division ATP-binding protein FtsE from Escherichia coli (strain K12) (see paper)
33% identity, 41% coverage: 29:237/509 of query aligns to 12:217/222 of P0A9R7
- K41 (= K58) mutation to R: Does not bind ATP.
- C49 (≠ T66) mutation to A: Prevents dimer formation. Does not alter ATP-binding.
8w6iD Cryo-em structure of escherichia coli str k12 ftsex complex with atp- gamma-s in peptidisc
33% identity, 41% coverage: 29:237/509 of query aligns to 12:217/219 of 8w6iD
- binding phosphothiophosphoric acid-adenylate ester: S37 (≠ N54), G38 (= G55), A39 (≠ C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), Q86 (= Q102), K130 (vs. gap), Q137 (≠ E157), S139 (≠ A159), G140 (≠ I160), G141 (≠ A161), E142 (≠ Q162), H195 (= H215)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
31% identity, 44% coverage: 20:241/509 of query aligns to 1:223/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F29), S35 (≠ N54), G36 (= G55), C37 (= C56), G38 (= G57), K39 (= K58), S40 (= S59), T41 (= T60), R126 (≠ L153), A130 (≠ E157), S132 (≠ A159), G134 (≠ A161), Q135 (= Q162)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
31% identity, 44% coverage: 20:241/509 of query aligns to 3:225/374 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)
31% identity, 44% coverage: 20:241/509 of query aligns to 3:225/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F29), S37 (≠ N54), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), Q81 (= Q102), R128 (≠ L153), A132 (≠ E157), S134 (≠ A159), G136 (≠ A161), Q137 (= Q162), E158 (= E183), H191 (= H215)
- binding magnesium ion: S42 (= S59), Q81 (= Q102)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
31% identity, 44% coverage: 20:241/509 of query aligns to 3:225/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F29), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), R128 (≠ L153), S134 (≠ A159), Q137 (= Q162)
- binding beryllium trifluoride ion: S37 (≠ N54), G38 (= G55), K41 (= K58), Q81 (= Q102), S134 (≠ A159), G136 (≠ A161), H191 (= H215)
- binding magnesium ion: S42 (= S59), Q81 (= Q102)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
31% identity, 44% coverage: 20:241/509 of query aligns to 3:225/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F29), V17 (≠ A34), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), R128 (≠ L153), A132 (≠ E157), S134 (≠ A159), Q137 (= Q162)
- binding tetrafluoroaluminate ion: S37 (≠ N54), G38 (= G55), K41 (= K58), Q81 (= Q102), S134 (≠ A159), G135 (≠ I160), G136 (≠ A161), E158 (= E183), H191 (= H215)
- binding magnesium ion: S42 (= S59), Q81 (= Q102)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
31% identity, 44% coverage: 20:241/509 of query aligns to 3:225/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F29), V17 (≠ A34), G38 (= G55), C39 (= C56), G40 (= G57), K41 (= K58), S42 (= S59), T43 (= T60), R128 (≠ L153), A132 (≠ E157), S134 (≠ A159), Q137 (= Q162)
- binding magnesium ion: S42 (= S59), Q81 (= Q102)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
31% identity, 44% coverage: 20:241/509 of query aligns to 4:226/371 of P68187
- A85 (= A105) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P126) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ M134) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I137) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G143) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ A161) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D182) 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.
8hd0A Cell divisome spg hydrolysis machinery ftsex-envc
32% identity, 41% coverage: 29:237/509 of query aligns to 12:217/218 of 8hd0A
Sites not aligning to the query:
2pclA Crystal structure of abc transporter with complex (aq_297) from aquifex aeolicus vf5
30% identity, 43% coverage: 19:237/509 of query aligns to 3:218/223 of 2pclA
1g6hA Crystal structure of the adp conformation of mj1267, an atp-binding cassette of an abc transporter (see paper)
31% identity, 46% coverage: 19:254/509 of query aligns to 4:243/254 of 1g6hA
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
30% identity, 43% coverage: 19:236/509 of query aligns to 1:220/343 of P30750
- 40:46 (vs. 54:60, 71% identical) binding
- E166 (= E183) 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
Query Sequence
>SM_b20485 FitnessBrowser__Smeli:SM_b20485
MGLDSMHQSASAASTDKPLLSLRNINMTFGGVKALKNVSFEVQPGEVHCLAGENGCGKST
LIKVITGVYRPAEGAVIEYDGETYPHMSPVTAQDRGIQVIWQDLALFPEMTVAENIAFHE
VLGGRPRLVDYGRMRRIAVDALGRLGITLDVDLPLKEYAIAQRQIVAIARALVGEAKLVF
MDEPTASLTQSETDHLLEIVRSLSASGVAVVFVSHRLAEVLEISSRITVLRDGALVGVYP
AAGMTQSKITELMTGKTFDQHVRARPRDDQPVVLDVRGLTRPGQFEDISFTVRRGETVGI
TGLLGAGRTEVALALFGMLKPATGTISIDGREVRFGSNREAIRAGVAYLSEDRLSLGLIQ
PQPIADNLVIASLRKILSGGLLSEDRKRSLVSRWIADLGVKIGHQADAISTLSGGNQQRV
AIAKWLATDPKLLILDSPTVGVDVGARAGIFDIVAKLAESGLAIILISDEVPEVYFNADR
VLHMAQGRIVGTYDPRQSRLEEIEAAVYA
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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