SitesBLAST
Comparing AZOBR_RS15495 FitnessBrowser__azobra:AZOBR_RS15495 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
38% identity, 98% coverage: 1:354/360 of query aligns to 2:366/375 of 2d62A
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
43% identity, 75% coverage: 14:282/360 of query aligns to 14:284/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
43% identity, 75% coverage: 14:282/360 of query aligns to 14:284/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
43% identity, 75% coverage: 14:282/360 of query aligns to 14:284/353 of 1oxuA
Sites not aligning to the query:
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)
43% identity, 75% coverage: 14:282/360 of query aligns to 14:284/353 of Q97UY8
- S142 (= S139) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G141) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E163) 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+).
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 94% coverage: 3:342/360 of query aligns to 1:354/371 of P68187
- A85 (= A91) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A118) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ T121) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ G123) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A128) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G141) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D162) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ A232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ R243) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (vs. gap) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (= G267) mutation to P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- S282 (≠ D271) mutation to L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G284 (≠ L273) mutation to S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G302 (= G292) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (≠ A298) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (≠ D318) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (vs. gap) 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.
Sites not aligning to the query:
- 355 F→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)
39% identity, 94% coverage: 5:342/360 of query aligns to 2:353/374 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)
38% identity, 94% coverage: 5:342/360 of query aligns to 2:353/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y15), S37 (= S40), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (≠ S46), Q81 (= Q88), R128 (≠ S133), A132 (≠ H137), S134 (= S139), G136 (= G141), Q137 (= Q142), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S45), Q81 (= Q88)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 94% coverage: 5:342/360 of query aligns to 2:353/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (≠ S46), R128 (≠ S133), S134 (= S139), Q137 (= Q142)
- binding beryllium trifluoride ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q88), S134 (= S139), G136 (= G141), H191 (= H196)
- binding magnesium ion: S42 (= S45), Q81 (= Q88)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 94% coverage: 5:342/360 of query aligns to 2:353/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (≠ S46), R128 (≠ S133), A132 (≠ H137), S134 (= S139), Q137 (= Q142)
- binding tetrafluoroaluminate ion: S37 (= S40), G38 (= G41), K41 (= K44), Q81 (= Q88), S134 (= S139), G135 (= G140), G136 (= G141), E158 (= E163), H191 (= H196)
- binding magnesium ion: S42 (= S45), Q81 (= Q88)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 94% coverage: 5:342/360 of query aligns to 2:353/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y15), V17 (≠ A20), G38 (= G41), C39 (= C42), G40 (= G43), K41 (= K44), S42 (= S45), T43 (≠ S46), R128 (≠ S133), A132 (≠ H137), S134 (= S139), Q137 (= Q142)
- binding magnesium ion: S42 (= S45), Q81 (= Q88)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 93% coverage: 8:342/360 of query aligns to 3:351/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ Y15), S35 (= S40), G36 (= G41), C37 (= C42), G38 (= G43), K39 (= K44), S40 (= S45), T41 (≠ S46), R126 (≠ S133), A130 (≠ H137), S132 (= S139), G134 (= G141), Q135 (= Q142)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 97% coverage: 3:350/360 of query aligns to 1:365/369 of P19566
- L86 (= L92) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P164) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D169) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (≠ A298) mutation to 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)
41% identity, 72% coverage: 24:282/360 of query aligns to 36:302/378 of P69874
- F45 (≠ I33) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C42) mutation to T: Loss of ATPase activity and transport.
- L60 (= L48) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I64) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V125) mutation to M: Loss of ATPase activity and transport.
- D172 (= D162) mutation to N: Loss of ATPase activity and transport.
- C276 (≠ V253) mutation to A: Lower ATPase activity and transport efficiency.
- E297 (= E277) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 26 C→A: Lower ATPase activity and transport efficiency.
- 27 F→L: Lower ATPase activity and transport efficiency.
1g291 Malk (see paper)
38% identity, 98% coverage: 3:354/360 of query aligns to 1:363/372 of 1g291
- binding magnesium ion: D69 (= D71), E71 (= E72), K72 (≠ R73), K79 (≠ E79), D80 (≠ R80), E292 (= E277), D293 (≠ A278), K359 (≠ Q350)
- binding pyrophosphate 2-: S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (≠ S45), T44 (≠ S46)
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 91% coverage: 6:332/360 of query aligns to 3:323/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
35% identity, 98% coverage: 6:357/360 of query aligns to 3:354/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y15), S38 (= S40), C40 (= C42), G41 (= G43), K42 (= K44), S43 (= S45), T44 (≠ S46), Q82 (= Q88), R129 (≠ S133), Q133 (≠ H137), S135 (= S139), G136 (= G140), G137 (= G141), Q159 (≠ E163), H192 (= H196)
- binding magnesium ion: S43 (= S45), Q82 (= Q88)
8hprC Lpqy-sugabc in state 4 (see paper)
37% identity, 89% coverage: 6:327/360 of query aligns to 3:320/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y15), S38 (= S40), G39 (= G41), G41 (= G43), K42 (= K44), S43 (= S45), Q82 (= Q88), Q133 (≠ H137), G136 (= G140), G137 (= G141), Q138 (= Q142), H192 (= H196)
- binding magnesium ion: S43 (= S45), Q82 (= Q88)
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
37% identity, 92% coverage: 5:336/360 of query aligns to 3:347/350 of 3fvqB
- binding adenosine-5'-triphosphate: F13 (≠ Y15), Q14 (≠ G16), T16 (≠ V18), V18 (≠ A20), S38 (= S40), G39 (= G41), C40 (= C42), G41 (= G43), K42 (= K44), T43 (≠ S45), T44 (≠ S46), R133 (≠ S133), E137 (≠ H137), S139 (= S139), G141 (= G141), Q142 (= Q142)
- binding calcium ion: T43 (≠ S45), Q86 (= Q88)
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, 61% coverage: 20:239/360 of query aligns to 19:236/393 of P9WQI3
- H193 (= H196) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
Query Sequence
>AZOBR_RS15495 FitnessBrowser__azobra:AZOBR_RS15495
ITMEALALNGVTHRYGRVVAVDDVSVTIGAGEIVCLCGPSGCGKSSLLRIAAGLEAVQTG
SVRIGGTVVADERGAVPPERRGVGLVFQDYALFPHLSVLDNVRFGLTALSGEAQRKRALE
TLGQVGMAGYADSFPHHLSGGQQQRVALARALAPNPAVLLLDEPFSGLDARLREQVRDET
LHVLKQNGAATMLVTHDPEEAMFLADRIALMRAGKVVQVGNPVDLYTRPVNAFAAEFFGE
VNRLSGVVQGGAVDTPVGPIPTEVADGTAVDVLIRPEALKLSAQPAATVPAGDLPVLARV
MAARLLGRTSLVHLDVPDGKGGSVHLHSRMPGQFLPPEQSHVSVCMDLCQAFVFPAGAPT
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