SitesBLAST
Comparing WP_011654139.1 NCBI__GCF_000009265.1:WP_011654139.1 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
44% identity, 95% coverage: 17:406/410 of query aligns to 2:380/382 of 7ahhC
- 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: L275 (≠ Q297), S297 (≠ E321), S298 (≠ Y322)
- binding phosphoaminophosphonic acid-adenylate ester: F12 (= F27), T39 (≠ S54), V40 (≠ I55), G41 (= G56), G62 (= G77), G64 (= G79), K65 (= K80), D187 (= D202), E188 (= E203)
7aheC Opua inhibited inward facing (see paper)
44% identity, 95% coverage: 17:406/410 of query aligns to 2:380/382 of 7aheC
- 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: L275 (≠ Q297), S297 (≠ E321), S298 (≠ Y322)
7ahdC Opua (e190q) occluded (see paper)
57% identity, 63% coverage: 17:275/410 of query aligns to 2:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F27), T39 (≠ S54), S61 (= S76), G62 (= G77), G64 (= G79), K65 (= K80), S66 (= S81), T67 (= T82), Q111 (= Q126), K161 (≠ D176), Q162 (= Q177), S164 (= S179), G166 (= G181), M167 (= M182), Q188 (≠ E203), H221 (= H236)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
39% identity, 55% coverage: 52:277/410 of query aligns to 17:242/375 of 2d62A
1g291 Malk (see paper)
39% identity, 58% coverage: 40:277/410 of query aligns to 2:239/372 of 1g291
- binding magnesium ion: D69 (≠ G107), E71 (≠ S109), K72 (≠ R110), K79 (≠ R117), D80 (≠ R118)
- binding pyrophosphate 2-: S38 (= S76), G39 (= G77), C40 (≠ S78), G41 (= G79), K42 (= K80), T43 (≠ S81), T44 (= T82)
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)
41% identity, 54% coverage: 64:283/410 of query aligns to 40:253/378 of P69874
- F45 (≠ I69) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S78) mutation to T: Loss of ATPase activity and transport.
- L60 (= L84) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I100) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V165) mutation to M: Loss of ATPase activity and transport.
- D172 (= D202) 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)
41% identity, 54% coverage: 64:283/410 of query aligns to 25:238/358 of 8y5iA
Sites not aligning to the query:
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 64% coverage: 18:280/410 of query aligns to 2:243/343 of P30750
- 40:46 (vs. 76:82, 86% identical) binding ATP
- E166 (= E203) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding L-methionine
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding L-methionine
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
36% identity, 64% coverage: 18:280/410 of query aligns to 3:244/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (= F27), Q14 (≠ A49), I19 (≠ S54), S41 (= S76), G42 (= G77), A43 (≠ S78), G44 (= G79), K45 (= K80), S46 (= S81), T47 (= T82), N141 (≠ Q177), S143 (= S179), Q146 (≠ M182), H200 (= H236)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
36% identity, 64% coverage: 18:280/410 of query aligns to 3:244/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
36% identity, 64% coverage: 18:280/410 of query aligns to 3:244/344 of 3tuiC
8hprC Lpqy-sugabc in state 4 (see paper)
41% identity, 59% coverage: 37:277/410 of query aligns to 5:233/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ K44), S38 (= S76), G39 (= G77), G41 (= G79), K42 (= K80), S43 (= S81), Q82 (= Q126), Q133 (= Q177), G136 (= G180), G137 (= G181), Q138 (≠ M182), H192 (= H236)
- binding magnesium ion: S43 (= S81), Q82 (= Q126)
8hprD Lpqy-sugabc in state 4 (see paper)
41% identity, 59% coverage: 37:277/410 of query aligns to 5:233/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ K44), S38 (= S76), C40 (≠ S78), G41 (= G79), K42 (= K80), S43 (= S81), T44 (= T82), Q82 (= Q126), R129 (≠ S173), Q133 (= Q177), S135 (= S179), G136 (= G180), G137 (= G181), Q159 (≠ E203), H192 (= H236)
- binding magnesium ion: S43 (= S81), Q82 (= Q126)
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 54% coverage: 57:278/410 of query aligns to 17:232/384 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)
41% identity, 54% coverage: 57:277/410 of query aligns to 20:234/393 of P9WQI3
- H193 (= H236) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
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, 56% coverage: 50:278/410 of query aligns to 11:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ T51), S37 (= S76), G38 (= G77), C39 (≠ S78), G40 (= G79), K41 (= K80), S42 (= S81), T43 (= T82), Q81 (= Q126), R128 (≠ S173), A132 (≠ Q177), S134 (= S179), G136 (= G181), Q137 (≠ M182), E158 (= E203), H191 (= H236)
- binding magnesium ion: S42 (= S81), Q81 (= Q126)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 56% coverage: 50:278/410 of query aligns to 11:233/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ T51), G38 (= G77), C39 (≠ S78), G40 (= G79), K41 (= K80), S42 (= S81), T43 (= T82), R128 (≠ S173), S134 (= S179), Q137 (≠ M182)
- binding beryllium trifluoride ion: S37 (= S76), G38 (= G77), K41 (= K80), Q81 (= Q126), S134 (= S179), G136 (= G181), H191 (= H236)
- binding magnesium ion: S42 (= S81), Q81 (= Q126)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 56% coverage: 50:278/410 of query aligns to 11:233/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ T51), V17 (≠ G56), G38 (= G77), C39 (≠ S78), G40 (= G79), K41 (= K80), S42 (= S81), T43 (= T82), R128 (≠ S173), A132 (≠ Q177), S134 (= S179), Q137 (≠ M182)
- binding tetrafluoroaluminate ion: S37 (= S76), G38 (= G77), K41 (= K80), Q81 (= Q126), S134 (= S179), G135 (= G180), G136 (= G181), E158 (= E203), H191 (= H236)
- binding magnesium ion: S42 (= S81), Q81 (= Q126)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 56% coverage: 50:278/410 of query aligns to 11:233/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ T51), V17 (≠ G56), G38 (= G77), C39 (≠ S78), G40 (= G79), K41 (= K80), S42 (= S81), T43 (= T82), R128 (≠ S173), A132 (≠ Q177), S134 (= S179), Q137 (≠ M182)
- binding magnesium ion: S42 (= S81), Q81 (= Q126)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
38% identity, 56% coverage: 50:278/410 of query aligns to 12:234/371 of P68187
- A85 (= A129) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G150) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A158) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A161) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ K163) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ D168) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G181) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D202) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D272) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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.
Query Sequence
>WP_011654139.1 NCBI__GCF_000009265.1:WP_011654139.1
MNSATGKDAPTQSATTKISLKNIYKVFGEHPKKAFALLRAGKTKSEIHAATGCSIGVNDA
SFDIRAGEIFVIMGLSGSGKSTLLRLLNRLIEPSSGSIEIDGRDITGMSRSELIALRRRD
ISMVFQSVALLPNRTVLNNAAFGLEVAGVGEAGRKQKALAALKAVGLDGYADSRPDQLSG
GMKQRVGLARALASEPTILLMDEAFSALDPLIRTEMQDELVRLQSEHSRTIVFVSHDLDE
AMRIGDRICIMQNGNVVQVGAPDEIVTQPANDYVRSFFRNVDVAHVFKAGDVARKSQVTI
IEREGVSAAAALERMKNYDREYAIILGRDKTYHGMISQTSLIEKMRAKAADPYRGAFLTE
IQAIPASEPLSNVLGKVAASPWPVPVVCDRNRYIGSISKSALLETLDRAS
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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