SitesBLAST
Comparing WP_084275096.1 NCBI__GCF_900176045.1:WP_084275096.1 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)
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 78% coverage: 7:210/262 of query aligns to 12:221/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y7), S38 (= S33), G39 (= G34), G41 (= G36), K42 (= K37), S43 (≠ T38), Q82 (= Q79), Q133 (= Q122), G136 (= G125), G137 (= G126), Q138 (= Q127), H192 (= H181)
- binding magnesium ion: S43 (≠ T38), Q82 (= Q79)
8hprD Lpqy-sugabc in state 4 (see paper)
40% identity, 78% coverage: 7:210/262 of query aligns to 12:221/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y7), S38 (= S33), C40 (≠ S35), G41 (= G36), K42 (= K37), S43 (≠ T38), T44 (= T39), Q82 (= Q79), R129 (= R118), Q133 (= Q122), S135 (= S124), G136 (= G125), G137 (= G126), Q159 (≠ E148), H192 (= H181)
- binding magnesium ion: S43 (≠ T38), Q82 (= Q79)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 79% coverage: 4:210/262 of query aligns to 10:230/375 of 2d62A
1g291 Malk (see paper)
38% identity, 74% coverage: 16:210/262 of query aligns to 21:227/372 of 1g291
- binding magnesium ion: D69 (≠ G63), E71 (≠ K65), K72 (≠ S66), K79 (≠ Q70), D80 (≠ K71)
- binding pyrophosphate 2-: S38 (= S33), G39 (= G34), C40 (≠ S35), G41 (= G36), K42 (= K37), T43 (= T38), T44 (= T39)
Sites not aligning to the query:
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 74% coverage: 16:210/262 of query aligns to 35:235/378 of P69874
- F45 (= F26) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S35) mutation to T: Loss of ATPase activity and transport.
- L60 (= L41) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ G57) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ T110) mutation to M: Loss of ATPase activity and transport.
- D172 (= D147) 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.
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 74% coverage: 16:210/262 of query aligns to 19:219/384 of 8hplC
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, 72% coverage: 7:194/262 of query aligns to 17:206/393 of P9WQI3
- H193 (= H181) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 72% coverage: 16:203/262 of query aligns to 23:221/353 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)
36% identity, 72% coverage: 16:203/262 of query aligns to 23:221/353 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)
36% identity, 72% coverage: 16:203/262 of query aligns to 23:221/353 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)
36% identity, 72% coverage: 16:203/262 of query aligns to 23:221/353 of Q97UY8
- S142 (= S124) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G126) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E148) 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+).
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
35% identity, 93% coverage: 14:256/262 of query aligns to 16:255/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S33), G36 (= G34), C37 (≠ S35), G38 (= G36), K39 (= K37), S40 (≠ T38), T41 (= T39), R126 (= R118), A130 (≠ Q122), S132 (= S124), G134 (= G126), Q135 (= Q127)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
35% identity, 93% coverage: 14:256/262 of query aligns to 18:257/374 of 2awnB
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)
35% identity, 93% coverage: 14:256/262 of query aligns to 18:257/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S33), G38 (= G34), C39 (≠ S35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (= T39), Q81 (= Q79), R128 (= R118), A132 (≠ Q122), S134 (= S124), G136 (= G126), Q137 (= Q127), E158 (= E148), H191 (= H181)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q79)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
35% identity, 93% coverage: 14:256/262 of query aligns to 18:257/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G34), C39 (≠ S35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (= T39), R128 (= R118), S134 (= S124), Q137 (= Q127)
- binding beryllium trifluoride ion: S37 (= S33), G38 (= G34), K41 (= K37), Q81 (= Q79), S134 (= S124), G136 (= G126), H191 (= H181)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q79)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
35% identity, 93% coverage: 14:256/262 of query aligns to 18:257/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G34), C39 (≠ S35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (= T39), R128 (= R118), A132 (≠ Q122), S134 (= S124), Q137 (= Q127)
- binding tetrafluoroaluminate ion: S37 (= S33), G38 (= G34), K41 (= K37), Q81 (= Q79), S134 (= S124), G135 (= G125), G136 (= G126), E158 (= E148), H191 (= H181)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q79)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
35% identity, 93% coverage: 14:256/262 of query aligns to 18:257/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G34), C39 (≠ S35), G40 (= G36), K41 (= K37), S42 (≠ T38), T43 (= T39), R128 (= R118), A132 (≠ Q122), S134 (= S124), Q137 (= Q127)
- binding magnesium ion: S42 (≠ T38), Q81 (= Q79)
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)
35% identity, 93% coverage: 14:256/262 of query aligns to 19:258/371 of P68187
- A85 (= A82) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R97) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I109) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D111) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ K116) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G126) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D147) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ E228) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ R239) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
37% identity, 72% coverage: 14:201/262 of query aligns to 19:212/369 of P19566
- L86 (= L83) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P149) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D154) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
38% identity, 72% coverage: 16:203/262 of query aligns to 24:209/353 of 1vciA
Sites not aligning to the query:
Query Sequence
>WP_084275096.1 NCBI__GCF_900176045.1:WP_084275096.1
MIAIGIYKELRDFSLEISMRVNEGEFIAITGASGSGKTTFLRVLAGLEEAKGAIVIGDEE
WLGNKSLPPQKRAVGFVFQDYALFPNMSVLQNLLFVRKDVALAMHLLKITDMLDLKDRYP
SQLSGGQKQRVALARAYMKKPKIMLLDEPLAALDPTIRSFLQGKIRDLHEEFGTTTFMVS
HDIAEIYRLSTRVIEIERGKILRDFTKDHIGKNKRSYKAEIVDVLQEEIVVAFMGDLFRL
PKKKTYKVGDIVEVTIEDLKLL
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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