SitesBLAST
Comparing AZOBR_RS27845 FitnessBrowser__azobra:AZOBR_RS27845 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)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
47% identity, 92% coverage: 10:344/365 of query aligns to 17:352/378 of P69874
- C26 (≠ Y19) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F20) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F38) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C47) mutation to T: Loss of ATPase activity and transport.
- L60 (= L53) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I69) 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 (≠ S263) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E284) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
1g291 Malk (see paper)
45% identity, 85% coverage: 13:321/365 of query aligns to 4:331/372 of 1g291
- binding magnesium ion: D69 (≠ R76), E71 (vs. gap), K72 (vs. gap), K79 (≠ H80), D80 (≠ R81), E292 (= E284), D293 (≠ H285)
- binding pyrophosphate 2-: S38 (= S45), G39 (= G46), C40 (= C47), G41 (= G48), K42 (= K49), T43 (= T50), T44 (= T51)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
48% identity, 67% coverage: 9:254/365 of query aligns to 5:258/375 of 2d62A
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
40% identity, 94% coverage: 11:354/365 of query aligns to 7:343/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 75% coverage: 16:287/365 of query aligns to 5:285/384 of 8hplC
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 75% coverage: 14:287/365 of query aligns to 7:287/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y19), S38 (= S45), G39 (= G46), G41 (= G48), K42 (= K49), S43 (≠ T50), Q82 (= Q89), Q133 (≠ E140), G136 (= G143), G137 (= G144), Q138 (= Q145), H192 (= H199)
- binding magnesium ion: S43 (≠ T50), Q82 (= Q89)
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 75% coverage: 14:287/365 of query aligns to 7:287/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y19), S38 (= S45), C40 (= C47), G41 (= G48), K42 (= K49), S43 (≠ T50), T44 (= T51), Q82 (= Q89), R129 (= R136), Q133 (≠ E140), S135 (= S142), G136 (= G143), G137 (= G144), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (≠ T50), Q82 (= Q89)
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, 85% coverage: 9:320/365 of query aligns to 2:318/369 of P19566
- L86 (= L93) 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.
- E306 (≠ I308) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 96% coverage: 9:360/365 of query aligns to 1:359/374 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)
36% identity, 96% coverage: 9:360/365 of query aligns to 1:359/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F20), S37 (= S45), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), Q81 (= Q89), R128 (= R136), A132 (≠ E140), S134 (= S142), G136 (= G144), Q137 (= Q145), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q89)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 96% coverage: 9:360/365 of query aligns to 1:359/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F20), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), R128 (= R136), S134 (= S142), Q137 (= Q145)
- binding beryllium trifluoride ion: S37 (= S45), G38 (= G46), K41 (= K49), Q81 (= Q89), S134 (= S142), G136 (= G144), H191 (= H199)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q89)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 96% coverage: 9:360/365 of query aligns to 1:359/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F20), V17 (≠ A25), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), R128 (= R136), A132 (≠ E140), S134 (= S142), Q137 (= Q145)
- binding tetrafluoroaluminate ion: S37 (= S45), G38 (= G46), K41 (= K49), Q81 (= Q89), S134 (= S142), G135 (= G143), G136 (= G144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q89)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 96% coverage: 9:360/365 of query aligns to 1:359/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F20), V17 (≠ A25), G38 (= G46), C39 (= C47), G40 (= G48), K41 (= K49), S42 (≠ T50), T43 (= T51), R128 (= R136), A132 (≠ E140), S134 (= S142), Q137 (= Q145)
- binding magnesium ion: S42 (≠ T50), Q81 (= Q89)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 96% coverage: 9:360/365 of query aligns to 2:360/371 of P68187
- A85 (= A92) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A113) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A121) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A124) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E126) 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 (= R235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L246) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ H268) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (≠ A279) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (vs. gap) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (vs. gap) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G302) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ I308) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ E322) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (= G340) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (= G346) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (≠ I355) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 96% coverage: 11:360/365 of query aligns to 1:357/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F20), S35 (= S45), G36 (= G46), C37 (= C47), G38 (= G48), K39 (= K49), S40 (≠ T50), T41 (= T51), R126 (= R136), A130 (≠ E140), S132 (= S142), G134 (= G144), Q135 (= Q145)
P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 64% coverage: 16:249/365 of query aligns to 9:245/393 of P9WQI3
- H193 (= H199) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
3d31A Modbc from methanosarcina acetivorans (see paper)
37% identity, 95% coverage: 10:355/365 of query aligns to 1:347/348 of 3d31A
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 92% coverage: 27:360/365 of query aligns to 12:329/344 of 2awnC
Sites not aligning to the query:
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
40% identity, 87% coverage: 9:325/365 of query aligns to 2:319/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (= F20), Q14 (≠ G21), T16 (≠ Y23), V18 (≠ A25), S38 (= S45), G39 (= G46), C40 (= C47), G41 (= G48), K42 (= K49), T43 (= T50), T44 (= T51), R133 (= R136), E137 (= E140), S139 (= S142), G141 (= G144), Q142 (= Q145)
- binding calcium ion: T43 (= T50), Q86 (= Q89)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
35% identity, 80% coverage: 13:304/365 of query aligns to 6:294/353 of 1oxvD
Query Sequence
>AZOBR_RS27845 FitnessBrowser__azobra:AZOBR_RS27845
MSATPKPDALLSIRSIDKYFGTYHALRDVSLDVAHGEFVALLGPSGCGKTTLLRCIAGFL
SPDSGTIRIGGEDVTRLPPHRRPLNTVFQHYALFPHLSILDNVAYGPRRHGVARGEALER
AREALELVGLDSAAGRHPRELSGGQQQRVALARAFVNRPKLLLLDEPLSALDLKLRKRMQ
IELKHLQEKLGIAFVFVTHDQEEAMSMANRIVVMNRGVIEQVGDGRAIYTRPASRFVADF
IGEANLLPGTAEGDAGVRLAVGSALLPHLGADTRQRYTAVLRPEHVELLKEPEAPGLITD
QGFVEDVIDTGGQTVVTVRVGEHLLASRRLGMAGEGLNPGAPVFVGFRPGHVHIIAEPAT
HRSGP
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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