SitesBLAST
Comparing RR42_RS27115 FitnessBrowser__Cup4G11:RR42_RS27115 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)
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
55% identity, 98% coverage: 3:238/242 of query aligns to 1:236/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (= F13), V16 (= V18), S36 (= S38), G37 (= G39), S38 (= S40), G39 (= G41), K40 (= K42), S41 (= S43), T42 (= T44), E162 (= E164), H194 (= H196)
- binding magnesium ion: S41 (= S43), E162 (= E164)
3c4jA Abc protein artp in complex with atp-gamma-s
53% identity, 98% coverage: 1:238/242 of query aligns to 1:238/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
53% identity, 98% coverage: 1:238/242 of query aligns to 1:238/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
53% identity, 98% coverage: 1:238/242 of query aligns to 1:238/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
53% identity, 98% coverage: 1:238/242 of query aligns to 1:238/242 of 2oljA
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
54% identity, 98% coverage: 3:238/242 of query aligns to 2:236/241 of 4u00A
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)
53% identity, 95% coverage: 8:238/242 of query aligns to 11:253/258 of P02915
- S41 (= S38) binding
- G42 (= G39) binding
- G44 (= G41) binding
- K45 (= K42) binding
- S46 (= S43) binding
- T47 (= T44) binding
1b0uA Atp-binding subunit of the histidine permease from salmonella typhimurium (see paper)
53% identity, 95% coverage: 8:238/242 of query aligns to 7:249/258 of 1b0uA
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 98% coverage: 3:238/242 of query aligns to 1:241/343 of P30750
- 40:46 (vs. 38:44, 86% identical) binding
- E166 (= E164) 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
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
43% identity, 98% coverage: 3:238/242 of query aligns to 2:242/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (= F13), Q14 (≠ A15), I19 (vs. gap), S41 (= S38), G42 (= G39), A43 (≠ S40), G44 (= G41), K45 (= K42), S46 (= S43), T47 (= T44), N141 (≠ Q138), S143 (= S140), Q146 (= Q143), H200 (= H196)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
43% identity, 98% coverage: 3:238/242 of query aligns to 2:242/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
43% identity, 98% coverage: 3:238/242 of query aligns to 2:242/344 of 3tuiC
5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
39% identity, 97% coverage: 1:234/242 of query aligns to 1:238/615 of 5lilA
- binding adenosine-5'-triphosphate: F13 (= F13), V22 (= V18), S42 (= S38), G43 (= G39), G45 (= G41), K46 (= K42), S47 (= S43), T48 (= T44), Q92 (= Q86), K136 (= K131), Q143 (= Q138), S145 (= S140), G147 (= G142), Q148 (= Q143)
- binding magnesium ion: S47 (= S43), Q92 (= Q86)
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
39% identity, 97% coverage: 1:234/242 of query aligns to 1:238/592 of 5lj7A
- binding adenosine-5'-triphosphate: V22 (= V18), S42 (= S38), G43 (= G39), G45 (= G41), K46 (= K42), S47 (= S43), T48 (= T44), Q92 (= Q86), K136 (= K131), Q143 (= Q138), S145 (= S140), G147 (= G142), Q148 (= Q143)
- binding magnesium ion: S47 (= S43), Q92 (= Q86)
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
40% identity, 91% coverage: 3:222/242 of query aligns to 4:226/648 of P75831
- K47 (= K42) mutation to L: Lack of activity.
- D169 (= D163) mutation to N: Lack of activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 99% coverage: 1:239/242 of query aligns to 1:235/371 of P68187
- A85 (≠ N89) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ C122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ A124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P232) 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.
5ws4A Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
40% identity, 96% coverage: 2:233/242 of query aligns to 3:230/650 of 5ws4A
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
36% identity, 99% coverage: 1:239/242 of query aligns to 1:235/369 of P19566
- L86 (= L90) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (≠ I165) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D170) 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.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 98% coverage: 3:239/242 of query aligns to 17:249/378 of P69874
- C26 (≠ R12) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F13) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ V31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S40) mutation to T: Loss of ATPase activity and transport.
- L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 98% coverage: 4:239/242 of query aligns to 3:234/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), S37 (= S38), G38 (= G39), C39 (≠ S40), G40 (= G41), K41 (= K42), S42 (= S43), T43 (= T44), Q81 (= Q86), R128 (≠ S134), A132 (≠ Q138), S134 (= S140), G136 (= G142), Q137 (= Q143), E158 (= E164), H191 (= H196)
- binding magnesium ion: S42 (= S43), Q81 (= Q86)
Query Sequence
>RR42_RS27115 FitnessBrowser__Cup4G11:RR42_RS27115
MSLIAIENVKKRFGANEVLKGIDLKVEAGEVIAIIGKSGSGKSTLLRCINGLESIDEGNI
TVAGAKLGSSELELRALRRKVGMIFQQFNLFPHLSAGRNVMLAPTVAAGVKEPEALTRAR
ECLAKVALAEKFDSYPDQLSGGQQQRVAIARALAMQPRALLCDEITSALDPELVVEVLNV
VRQLAREGMTLLMVTHEMRFAREVCNRVVFMHQGRVHEIGPPEQLFSHPATPELQQFLGM
AA
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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