SitesBLAST
Comparing Echvi_3653 Echvi_3653 ABC-type sulfate/molybdate transport systems, ATPase component 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
43% identity, 70% coverage: 20:222/290 of query aligns to 24:231/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 70% coverage: 21:222/290 of query aligns to 36:236/378 of P69874
- F45 (= F30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ M121) 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.
1g291 Malk (see paper)
37% identity, 90% coverage: 20:281/290 of query aligns to 21:290/372 of 1g291
- binding magnesium ion: D69 (= D68), E71 (≠ S70), K72 (≠ F71), K79 (≠ G78), D80 (≠ R79)
- binding pyrophosphate 2-: S38 (= S37), G39 (= G38), C40 (≠ S39), G41 (= G40), K42 (= K41), T43 (= T42), T44 (≠ S43)
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
35% identity, 89% coverage: 20:276/290 of query aligns to 18:267/348 of 3d31A
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)
40% identity, 77% coverage: 1:222/290 of query aligns to 1:222/371 of P68187
- A85 (≠ S90) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (= K111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (vs. gap) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L117) 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 (≠ L124) 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.
Sites not aligning to the query:
- 228 R→C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 241 F→I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- 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.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
40% identity, 76% coverage: 3:222/290 of query aligns to 2:221/374 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)
40% identity, 76% coverage: 3:222/290 of query aligns to 2:221/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ N13), S37 (= S37), G38 (= G38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), Q81 (= Q87), R128 (≠ T129), A132 (≠ H133), S134 (= S135), G136 (= G137), Q137 (= Q138), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q87)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 76% coverage: 3:222/290 of query aligns to 2:221/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ N13), G38 (= G38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (≠ T129), S134 (= S135), Q137 (= Q138)
- binding beryllium trifluoride ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q87), S134 (= S135), G136 (= G137), H191 (= H192)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q87)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 76% coverage: 3:222/290 of query aligns to 2:221/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ N13), V17 (vs. gap), G38 (= G38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (≠ T129), A132 (≠ H133), S134 (= S135), Q137 (= Q138)
- binding tetrafluoroaluminate ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q87), S134 (= S135), G135 (= G136), G136 (= G137), E158 (= E159), H191 (= H192)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q87)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 76% coverage: 3:222/290 of query aligns to 2:221/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ N13), V17 (vs. gap), G38 (= G38), C39 (≠ S39), G40 (= G40), K41 (= K41), S42 (≠ T42), T43 (≠ S43), R128 (≠ T129), A132 (≠ H133), S134 (= S135), Q137 (= Q138)
- binding magnesium ion: S42 (≠ T42), Q81 (= Q87)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 76% coverage: 4:222/290 of query aligns to 1:219/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ N13), S35 (= S37), G36 (= G38), C37 (≠ S39), G38 (= G40), K39 (= K41), S40 (≠ T42), T41 (≠ S43), R126 (≠ T129), A130 (≠ H133), S132 (= S135), G134 (= G137), Q135 (= Q138)
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 77% coverage: 1:222/290 of query aligns to 1:222/369 of P19566
- L86 (= L91) 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.
Sites not aligning to the query:
- 306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
38% identity, 78% coverage: 16:240/290 of query aligns to 20:247/353 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)
38% identity, 78% coverage: 16:240/290 of query aligns to 20:247/353 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)
38% identity, 78% coverage: 16:240/290 of query aligns to 20:247/353 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)
38% identity, 78% coverage: 16:240/290 of query aligns to 20:247/353 of Q97UY8
- S142 (= S135) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G137) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E159) 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+).
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)
40% identity, 70% coverage: 20:222/290 of query aligns to 22:223/393 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.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
35% identity, 75% coverage: 21:238/290 of query aligns to 20:240/240 of 4ymuJ
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
39% identity, 71% coverage: 20:224/290 of query aligns to 19:222/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
39% identity, 71% coverage: 20:224/290 of query aligns to 21:224/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S37), C40 (≠ S39), G41 (= G40), K42 (= K41), S43 (≠ T42), T44 (≠ S43), Q82 (= Q87), R129 (≠ T129), Q133 (≠ H133), S135 (= S135), G136 (= G136), G137 (= G137), Q159 (≠ E159), H192 (= H192)
- binding magnesium ion: S43 (≠ T42), Q82 (= Q87)
Sites not aligning to the query:
Query Sequence
>Echvi_3653 Echvi_3653 ABC-type sulfate/molybdate transport systems, ATPase component
MINIDLQKSLKANGPAMDLDIKLTISQGEFITLFGPSGSGKTSTLRMISGLLTPDKGHLS
VNGEQWFDASFGKNVSPGRRKLGYLFQDYSLFPNMTVKENIAFALKNAKDKAYLMELLES
MGLLHLQDTLPKHLSGGQQQRVALARALALKPDILLLDEPLSALDPSMREKLQEYILAIH
RKYALTTILVSHDAGEIIKLSDRIIELDHGKVLRQCTPKEFFGTGLTSAKFQFQGEIMDI
LEDDVVHIVHVKTGNDLVKVVCDMDETKELGVGDKVLVGSKAFNPLIKKL
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