SitesBLAST
Comparing 3609758 Dshi_3141 ABC transporter related (RefSeq) 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)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
51% identity, 99% coverage: 1:350/352 of query aligns to 4:374/375 of 2d62A
1g291 Malk (see paper)
50% identity, 99% coverage: 1:350/352 of query aligns to 1:371/372 of 1g291
- binding magnesium ion: D69 (= D69), E71 (vs. gap), K72 (vs. gap), K79 (= K73), D80 (= D74), E292 (≠ D277), D293 (= D278), K359 (≠ H338)
- binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
48% identity, 99% coverage: 1:350/352 of query aligns to 4:352/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
61% identity, 70% coverage: 2:248/352 of query aligns to 1:248/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ W13), S38 (= S38), G39 (= G39), G41 (= G41), K42 (= K42), S43 (≠ T43), Q82 (= Q82), Q133 (≠ A133), G136 (= G136), G137 (= G137), Q138 (= Q138), H192 (= H192)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q82)
8hprD Lpqy-sugabc in state 4 (see paper)
61% identity, 70% coverage: 2:248/352 of query aligns to 1:248/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ W13), S38 (= S38), C40 (= C40), G41 (= G41), K42 (= K42), S43 (≠ T43), T44 (= T44), Q82 (= Q82), R129 (= R129), Q133 (≠ A133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (≠ T43), Q82 (= Q82)
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)
56% identity, 80% coverage: 1:280/352 of query aligns to 1:288/393 of P9WQI3
- H193 (= H192) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
61% identity, 70% coverage: 2:248/352 of query aligns to 1:246/384 of 8hplC
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
43% identity, 98% coverage: 1:345/352 of query aligns to 1:356/369 of P19566
- L86 (= L86) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P160) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D165) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- E306 (= E297) mutation to K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
43% identity, 98% coverage: 1:345/352 of query aligns to 1:358/371 of P68187
- A85 (≠ G85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ L228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ L241) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (≠ I271) mutation to G: Normal maltose transport but constitutive mal gene expression.
- G278 (vs. gap) 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 (vs. gap) mutation to D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- E308 (= E297) mutation to Q: Maltose transport is affected but retains ability to interact with MalT.
- S322 (vs. gap) mutation to F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G340 (≠ D327) mutation to A: Maltose transport is affected but retains ability to interact with MalT.
- G346 (≠ S333) mutation to S: Normal maltose transport but constitutive mal gene expression.
- F355 (= F342) mutation to 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)
43% identity, 98% coverage: 2:345/352 of query aligns to 1:357/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (= W13), S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), Q81 (= Q82), R128 (= R129), A132 (= A133), S134 (= S135), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
43% identity, 98% coverage: 2:345/352 of query aligns to 1:357/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (= W13), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R129), S134 (= S135), Q137 (= Q138)
- binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
43% identity, 98% coverage: 2:345/352 of query aligns to 1:357/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (= W13), V17 (≠ G18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R129), A132 (= A133), S134 (= S135), Q137 (= Q138)
- binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q82), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
43% identity, 98% coverage: 2:345/352 of query aligns to 1:357/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (= W13), V17 (≠ G18), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R129), A132 (= A133), S134 (= S135), Q137 (= Q138)
- binding magnesium ion: S42 (≠ T43), Q81 (= Q82)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
43% identity, 98% coverage: 2:345/352 of query aligns to 1:357/374 of 2awnB
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
43% identity, 97% coverage: 4:345/352 of query aligns to 1:355/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (= W13), S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (≠ T43), T41 (= T44), R126 (= R129), A130 (= A133), S132 (= S135), G134 (= G137), Q135 (= Q138)
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
55% identity, 63% coverage: 24:246/352 of query aligns to 38:258/378 of P69874
- F45 (= F31) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C40) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M46) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) mutation to N: 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.
- 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.
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 92% coverage: 23:345/352 of query aligns to 15:327/344 of 2awnC
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 84% coverage: 1:294/352 of query aligns to 1:306/353 of 1oxvD
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 84% coverage: 1:294/352 of query aligns to 1:306/353 of 1oxvA
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
40% identity, 84% coverage: 1:294/352 of query aligns to 1:306/353 of 1oxuA
Query Sequence
>3609758 Dshi_3141 ABC transporter related (RefSeq)
MAEVILKDLTKRWGDFVGVDNQSLHVRDEEFLVLLGPSGCGKTTTMRMIAGLEDPTDGEI
WIGDRMVNDDLPKDRDVAMVFQNYGLYPHMTIFENIAYPLRVRGVDKAEIPPRVQRAAEQ
VELTKFLHRKPKALSGGQRQRVALARAIVRKPKVFLMDEPLSNLDAKLRVTMRAELKHLS
RELQITTVYVTHDQIEAMTLADRVAVMKHGVIQQLGTPDEIYNDPANLFVAGFIGSPAMN
LINGSVEDGMFVTTGGTRLVKVPSPDRARAILGVRADDMQVHEAGQGDIDVTIYAFENTG
ESTLLTVQWGKQRVIARGDRHLRKEQDDVVGISLNTDHLYLFDPDTEERIRM
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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