SitesBLAST
Comparing WP_109941010.1 NCBI__GCF_003173335.1:WP_109941010.1 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)
3d31A Modbc from methanosarcina acetivorans (see paper)
47% identity, 100% coverage: 1:209/209 of query aligns to 1:208/348 of 3d31A
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)
43% identity, 91% coverage: 16:206/209 of query aligns to 33:225/378 of P69874
- F45 (≠ W28) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S37) mutation to T: Loss of ATPase activity and transport.
- L60 (= L43) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L59) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L116) mutation to M: Loss of ATPase activity and transport.
- D172 (= D153) 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.
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
42% identity, 91% coverage: 16:206/209 of query aligns to 18:210/358 of 8y5iA
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)
42% identity, 89% coverage: 20:205/209 of query aligns to 24:211/393 of P9WQI3
- H193 (= H187) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
42% identity, 100% coverage: 2:209/209 of query aligns to 7:209/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 89% coverage: 20:206/209 of query aligns to 21:209/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
40% identity, 89% coverage: 20:206/209 of query aligns to 23:211/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S35), C40 (≠ S37), G41 (= G38), K42 (= K39), S43 (≠ T40), T44 (≠ V41), Q82 (= Q79), R129 (= R124), Q133 (= Q128), S135 (= S130), G136 (= G131), G137 (= G132), Q159 (≠ E154), H192 (= H187)
- binding magnesium ion: S43 (≠ T40), Q82 (= Q79)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 89% coverage: 20:206/209 of query aligns to 23:211/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S35), G39 (= G36), G41 (= G38), K42 (= K39), S43 (≠ T40), Q82 (= Q79), Q133 (= Q128), G136 (= G131), G137 (= G132), Q138 (≠ E133), H192 (= H187)
- binding magnesium ion: S43 (≠ T40), Q82 (= Q79)
Sites not aligning to the query:
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, 91% coverage: 20:209/209 of query aligns to 23:214/369 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 (= P155) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D160) 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.
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
41% identity, 90% coverage: 20:207/209 of query aligns to 26:221/375 of 2d62A
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
41% identity, 91% coverage: 20:209/209 of query aligns to 23:214/371 of P68187
- A85 (≠ S82) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P103) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ Y112) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ R114) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D119) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G132) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D153) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
41% identity, 91% coverage: 20:209/209 of query aligns to 22:213/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S35), G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ V41), Q81 (= Q79), R128 (= R124), A132 (≠ Q128), S134 (= S130), G136 (= G132), Q137 (≠ E133), E158 (= E154), H191 (= H187)
- binding magnesium ion: S42 (≠ T40), 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)
41% identity, 91% coverage: 20:209/209 of query aligns to 22:213/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ V41), R128 (= R124), S134 (= S130), Q137 (≠ E133)
- binding beryllium trifluoride ion: S37 (= S35), G38 (= G36), K41 (= K39), Q81 (= Q79), S134 (= S130), G136 (= G132), H191 (= H187)
- binding magnesium ion: S42 (≠ T40), 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)
41% identity, 91% coverage: 20:209/209 of query aligns to 22:213/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ V41), R128 (= R124), A132 (≠ Q128), S134 (= S130), Q137 (≠ E133)
- binding tetrafluoroaluminate ion: S37 (= S35), G38 (= G36), K41 (= K39), Q81 (= Q79), S134 (= S130), G135 (= G131), G136 (= G132), E158 (= E154), H191 (= H187)
- binding magnesium ion: S42 (≠ T40), 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)
41% identity, 91% coverage: 20:209/209 of query aligns to 22:213/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ V41), R128 (= R124), A132 (≠ Q128), S134 (= S130), Q137 (≠ E133)
- binding magnesium ion: S42 (≠ T40), Q81 (= Q79)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
41% identity, 91% coverage: 20:209/209 of query aligns to 20:211/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S35), G36 (= G36), C37 (≠ S37), G38 (= G38), K39 (= K39), S40 (≠ T40), T41 (≠ V41), R126 (= R124), A130 (≠ Q128), S132 (= S130), G134 (= G132), Q135 (≠ E133)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
41% identity, 91% coverage: 20:209/209 of query aligns to 22:213/374 of 2awnB
Sites not aligning to the query:
1g291 Malk (see paper)
41% identity, 89% coverage: 20:205/209 of query aligns to 23:216/372 of 1g291
- binding magnesium ion: D69 (= D60), E71 (≠ A62), K72 (≠ D63), K79 (≠ E70), D80 (≠ K71)
- binding pyrophosphate 2-: S38 (= S35), G39 (= G36), C40 (≠ S37), G41 (= G38), K42 (= K39), T43 (= T40), T44 (≠ V41)
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
39% identity, 91% coverage: 20:209/209 of query aligns to 46:243/382 of 7ahhC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
39% identity, 91% coverage: 20:209/209 of query aligns to 46:243/382 of 7aheC
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 275, 297, 298
Query Sequence
>WP_109941010.1 NCBI__GCF_003173335.1:WP_109941010.1
MIRIRDLLVRVGSFELPVKNLDVSDNDWVVITGRSGSGKTVFLETIAGFFKPESGSIILD
GADITSLPPEKRGISIVFQDYSLFPHMTARENIGYGLKLRNNPEIHSIVSDYARMLGIDS
LLDRSPAQLSGGEKQRVAIARALVVNPKLLLLDEPASALDHETRRSLWNDLCSLHDRGDL
TIIHVTHDRNEAEVLGNRRIIIDGGKFVE
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