SitesBLAST
Comparing HSERO_RS11145 FitnessBrowser__HerbieS:HSERO_RS11145 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
46% identity, 81% coverage: 18:308/359 of query aligns to 23:324/378 of P69874
- C26 (≠ R21) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F22) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ M40) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C49) mutation to T: Loss of ATPase activity and transport.
- L60 (= L55) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ A71) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V128) mutation to M: Loss of ATPase activity and transport.
- D172 (= D165) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ L264) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E283) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
44% identity, 74% coverage: 20:286/359 of query aligns to 14:298/375 of 2d62A
1g291 Malk (see paper)
45% identity, 71% coverage: 17:270/359 of query aligns to 8:271/372 of 1g291
- binding magnesium ion: D69 (≠ Q78), E71 (vs. gap), K72 (vs. gap), K79 (≠ Q82), D80 (≠ A83)
- binding pyrophosphate 2-: S38 (= S47), G39 (= G48), C40 (= C49), G41 (= G50), K42 (= K51), T43 (= T52), T44 (= T53)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
44% identity, 71% coverage: 11:265/359 of query aligns to 5:247/353 of 1vciA
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 78% coverage: 11:290/359 of query aligns to 2:286/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 78% coverage: 11:290/359 of query aligns to 2:286/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 78% coverage: 11:290/359 of query aligns to 2:286/353 of 1oxuA
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)
40% identity, 78% coverage: 11:290/359 of query aligns to 2:286/353 of Q97UY8
- S142 (= S142) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G144) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E166) 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+).
3d31A Modbc from methanosarcina acetivorans (see paper)
37% identity, 90% coverage: 12:335/359 of query aligns to 1:328/348 of 3d31A
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
45% identity, 66% coverage: 13:248/359 of query aligns to 3:242/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 66% coverage: 13:248/359 of query aligns to 4:243/371 of P68187
- A85 (= A94) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ Q115) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V121) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M124) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ S126) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D131) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G144) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D165) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ P235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ W246) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
45% identity, 66% coverage: 13:248/359 of query aligns to 3:242/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F22), S37 (= S47), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), Q81 (= Q91), R128 (≠ K136), A132 (≠ Q140), S134 (= S142), G136 (= G144), Q137 (= Q145), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q91)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
45% identity, 66% coverage: 13:248/359 of query aligns to 3:242/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F22), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ K136), S134 (= S142), Q137 (= Q145)
- binding beryllium trifluoride ion: S37 (= S47), G38 (= G48), K41 (= K51), Q81 (= Q91), S134 (= S142), G136 (= G144), H191 (= H199)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q91)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
45% identity, 66% coverage: 13:248/359 of query aligns to 3:242/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F22), V17 (≠ A27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ K136), A132 (≠ Q140), S134 (= S142), Q137 (= Q145)
- binding tetrafluoroaluminate ion: S37 (= S47), G38 (= G48), K41 (= K51), Q81 (= Q91), S134 (= S142), G135 (= G143), G136 (= G144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q91)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
45% identity, 66% coverage: 13:248/359 of query aligns to 3:242/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F22), V17 (≠ A27), G38 (= G48), C39 (= C49), G40 (= G50), K41 (= K51), S42 (≠ T52), T43 (= T53), R128 (≠ K136), A132 (≠ Q140), S134 (= S142), Q137 (= Q145)
- binding magnesium ion: S42 (≠ T52), Q81 (= Q91)
8hplC Lpqy-sugabc in state 1 (see paper)
45% identity, 63% coverage: 27:251/359 of query aligns to 16:244/384 of 8hplC
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
45% identity, 66% coverage: 13:248/359 of query aligns to 1:240/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F22), S35 (= S47), G36 (= G48), C37 (= C49), G38 (= G50), K39 (= K51), S40 (≠ T52), T41 (= T53), R126 (≠ K136), A130 (≠ Q140), S132 (= S142), G134 (= G144), Q135 (= Q145)
8hprC Lpqy-sugabc in state 4 (see paper)
45% identity, 63% coverage: 27:251/359 of query aligns to 18:246/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S47), G39 (= G48), G41 (= G50), K42 (= K51), S43 (≠ T52), Q82 (= Q91), Q133 (= Q140), G136 (= G143), G137 (= G144), Q138 (= Q145), H192 (= H199)
- binding magnesium ion: S43 (≠ T52), Q82 (= Q91)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
45% identity, 63% coverage: 27:251/359 of query aligns to 18:246/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S47), C40 (= C49), G41 (= G50), K42 (= K51), S43 (≠ T52), T44 (= T53), Q82 (= Q91), R129 (≠ K136), Q133 (= Q140), S135 (= S142), G136 (= G143), G137 (= G144), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (≠ T52), Q82 (= Q91)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
45% identity, 66% coverage: 13:248/359 of query aligns to 4:243/369 of P19566
- L86 (= L95) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P167) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D172) 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.
Query Sequence
>HSERO_RS11145 FitnessBrowser__HerbieS:HSERO_RS11145
MTAATEEDAAVFLSVREVEKRFGSFTALDRVSLEVRRGEMVCLLGPSGCGKTTLLRTIAG
LERQDSGRLHADGRDISQLPPQARDYGILFQSYALFPNLSVADNVAYGLGRMSRQQKRER
VTEMLSMVGLDGSQDKYPGQLSGGQQQRVALARALAPSPSLLLLDEPLSALDAQVREHLQ
LEIRRLQKQFRITTLMVTHDQEEAMVMADRIAVMQHGRIEQFGTPEQIYRRPATPFVADF
IGQANWLPFTRLSGSQVAVGGLHLEIQPDESDRASGRLFCRPEAVQLFSDESCANRFLAR
VVDRIYLGDRYRLALAADALPGQTLLADVSSQAHERVASLDTQDGLWVTLPRQSLQVFA
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