SitesBLAST
Comparing AZOBR_RS25880 FitnessBrowser__azobra:AZOBR_RS25880 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
36% identity, 93% coverage: 21:355/362 of query aligns to 18:370/375 of 2d62A
1g291 Malk (see paper)
38% identity, 92% coverage: 24:355/362 of query aligns to 18:367/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ E79), D80 (≠ A80), Y228 (≠ F229), D229 (≠ E230), E292 (= E287), D293 (vs. gap), S341 (≠ P329), E342 (= E330), K359 (≠ M347)
- binding pyrophosphate 2-: P37 (= P43), S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (= T49), T44 (= T50)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
37% identity, 92% coverage: 24:355/362 of query aligns to 21:348/353 of 1vciA
Sites not aligning to the query:
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)
43% identity, 70% coverage: 1:255/362 of query aligns to 1:249/393 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.
8hplC ABC transporter, ATP-binding protein SugC (see paper)
40% identity, 73% coverage: 24:287/362 of query aligns to 16:282/384 of 8hplC
Sites not aligning to the query:
8hprC ABC transporter, ATP-binding protein SugC (see paper)
40% identity, 73% coverage: 24:287/362 of query aligns to 18:284/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), S43 (≠ T49), T44 (= T50), Q82 (= Q88), G132 (≠ R138), Q133 (≠ N139), L134 (= L140), S135 (≠ T141), G136 (≠ A142), G137 (≠ D143), Q138 (≠ A144), H192 (= H199)
- binding magnesium ion: S43 (≠ T49), Q82 (= Q88)
Sites not aligning to the query:
8hprD ABC transporter, ATP-binding protein SugC (see paper)
40% identity, 73% coverage: 24:287/362 of query aligns to 18:284/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (≠ T49), T44 (= T50), Q82 (= Q88), R129 (= R135), G132 (≠ R138), Q133 (≠ N139), S135 (≠ T141), G136 (≠ A142), G137 (≠ D143), Q138 (≠ A144), Q159 (≠ E166), H192 (= H199)
- binding magnesium ion: S43 (≠ T49), Q82 (= Q88), D158 (= D165)
Sites not aligning to the query:
2awoA Crystal structure of the adp-mg-bound e. Coli malk (crystallized with adp-mg) (see paper)
34% identity, 89% coverage: 34:355/362 of query aligns to 27:359/372 of 2awoA
Sites not aligning to the query:
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
34% identity, 89% coverage: 34:355/362 of query aligns to 27:359/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: P36 (= P43), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), Q81 (= Q88), R128 (= R135), A132 (≠ N139), S134 (≠ T141), G135 (≠ A142), G136 (≠ D143), Q137 (≠ A144), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88), D157 (= D165)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
34% identity, 89% coverage: 34:355/362 of query aligns to 27:359/371 of 3puxA
- binding adenosine-5'-diphosphate: S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R135), A132 (≠ N139), L133 (= L140), S134 (≠ T141), Q137 (≠ A144)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (≠ T141), G135 (≠ A142), G136 (≠ D143), E158 (= E166), H191 (= H199)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88), D157 (= D165)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
34% identity, 89% coverage: 34:355/362 of query aligns to 27:359/371 of 3puwA
- binding adenosine-5'-diphosphate: S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (≠ T49), T43 (= T50), R128 (= R135), A132 (≠ N139), S134 (≠ T141), Q137 (≠ A144)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q88), S134 (≠ T141), G135 (≠ A142), G136 (≠ D143), E158 (= E166), N162 (≠ V170), H191 (= H199)
- binding magnesium ion: S42 (≠ T49), Q81 (= Q88)
Sites not aligning to the query:
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
34% identity, 89% coverage: 34:355/362 of query aligns to 28:360/371 of P68187
- A85 (≠ V91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I123) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G125) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T130) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (≠ D143) 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 (≠ V235) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ V248) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ A266) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G277) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ E281) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (= G283) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (≠ V301) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ D307) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ G321) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (≠ E338) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (vs. gap) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (≠ Y351) mutation to Y: Maltose transport is affected but retains ability to interact with MalT.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
34% identity, 89% coverage: 34:355/362 of query aligns to 27:359/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
34% identity, 89% coverage: 34:355/362 of query aligns to 25:357/367 of 1q12A