SitesBLAST
Comparing WP_011385763.1 NCBI__GCF_000009985.1:WP_011385763.1 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)
3d31A Modbc from methanosarcina acetivorans (see paper)
32% identity, 98% coverage: 1:354/363 of query aligns to 1:344/348 of 3d31A
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
35% identity, 61% coverage: 3:223/363 of query aligns to 24:234/375 of 2d62A
1g291 Malk (see paper)
38% identity, 54% coverage: 28:223/363 of query aligns to 34:231/372 of 1g291
- binding magnesium ion: D69 (= D63), E71 (≠ R65), K72 (≠ S66), K79 (≠ E73), D80 (≠ A74)
- binding pyrophosphate 2-: S38 (= S32), G39 (= G33), C40 (≠ S34), G41 (= G35), K42 (= K36), T43 (= T37), T44 (≠ S38)
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)
38% identity, 59% coverage: 3:217/363 of query aligns to 20:219/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S32), G38 (= G33), C39 (≠ S34), G40 (= G35), K41 (= K36), S42 (≠ T37), T43 (≠ S38), Q81 (= Q82), R128 (= R127), A132 (≠ K131), S134 (= S133), G136 (= G135), Q137 (≠ E136), E158 (= E157), H191 (= H190)
- binding magnesium ion: S42 (≠ T37), Q81 (= Q82)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
38% identity, 59% coverage: 3:217/363 of query aligns to 20:219/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G33), C39 (≠ S34), G40 (= G35), K41 (= K36), S42 (≠ T37), T43 (≠ S38), R128 (= R127), S134 (= S133), Q137 (≠ E136)
- binding beryllium trifluoride ion: S37 (= S32), G38 (= G33), K41 (= K36), Q81 (= Q82), S134 (= S133), G136 (= G135), H191 (= H190)
- binding magnesium ion: S42 (≠ T37), Q81 (= Q82)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
38% identity, 59% coverage: 3:217/363 of query aligns to 20:219/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G33), C39 (≠ S34), G40 (= G35), K41 (= K36), S42 (≠ T37), T43 (≠ S38), R128 (= R127), A132 (≠ K131), S134 (= S133), Q137 (≠ E136)
- binding tetrafluoroaluminate ion: S37 (= S32), G38 (= G33), K41 (= K36), Q81 (= Q82), S134 (= S133), G135 (= G134), G136 (= G135), E158 (= E157), H191 (= H190)
- binding magnesium ion: S42 (≠ T37), Q81 (= Q82)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
38% identity, 59% coverage: 3:217/363 of query aligns to 20:219/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G33), C39 (≠ S34), G40 (= G35), K41 (= K36), S42 (≠ T37), T43 (≠ S38), R128 (= R127), A132 (≠ K131), S134 (= S133), Q137 (≠ E136)
- binding magnesium ion: S42 (≠ T37), Q81 (= Q82)
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)
38% identity, 59% coverage: 3:217/363 of query aligns to 21:220/371 of P68187
- A85 (≠ R85) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ A106) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ L112) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V115) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E117) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E122) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G135) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D156) 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)
38% identity, 59% coverage: 3:217/363 of query aligns to 20:219/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
31% identity, 93% coverage: 3:340/363 of query aligns to 18:325/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S32), G36 (= G33), C37 (≠ S34), G38 (= G35), K39 (= K36), S40 (≠ T37), T41 (≠ S38), R126 (= R127), A130 (≠ K131), S132 (= S133), G134 (= G135), Q135 (≠ E136)
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)
39% identity, 59% coverage: 3:217/363 of query aligns to 21:220/369 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 (= P158) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D163) 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.
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)
34% identity, 73% coverage: 3:268/363 of query aligns to 22:261/393 of P9WQI3
- H193 (= H190) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
34% identity, 58% coverage: 14:223/363 of query aligns to 35:239/378 of P69874
- F45 (≠ G24) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S34) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ I40) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F62) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ L119) mutation to M: Loss of ATPase activity and transport.
- D172 (= D156) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
37% identity, 58% coverage: 5:214/363 of query aligns to 11:211/353 of 1vciA
8hprC Lpqy-sugabc in state 4 (see paper)
34% identity, 61% coverage: 5:224/363 of query aligns to 14:226/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S32), G39 (= G33), G41 (= G35), K42 (= K36), S43 (≠ T37), Q82 (= Q82), Q133 (≠ K131), G136 (= G134), G137 (= G135), Q138 (≠ E136), H192 (= H190)
- binding magnesium ion: S43 (≠ T37), Q82 (= Q82)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
34% identity, 61% coverage: 5:224/363 of query aligns to 14:226/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S32), C40 (≠ S34), G41 (= G35), K42 (= K36), S43 (≠ T37), T44 (≠ S38), Q82 (= Q82), R129 (= R127), Q133 (≠ K131), S135 (= S133), G136 (= G134), G137 (= G135), Q159 (≠ E157), H192 (= H190)
- binding magnesium ion: S43 (≠ T37), Q82 (= Q82)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
35% identity, 54% coverage: 28:224/363 of query aligns to 32:224/384 of 8hplC
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 59% coverage: 3:217/363 of query aligns to 13:189/344 of 2awnC
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)
35% identity, 57% coverage: 25:232/363 of query aligns to 33:240/343 of P30750
- 40:46 (vs. 32:38, 57% identical) binding
- E166 (= E157) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
34% identity, 57% coverage: 25:232/363 of query aligns to 34:241/344 of 3tuzC
Sites not aligning to the query:
Query Sequence
>WP_011385763.1 NCBI__GCF_000009985.1:WP_011385763.1
MLDLDLRRRQGEFRLDVRLSAGPGVTALYGRSGSGKTSVINMVAGLSRPDEGSISVDGRV
LFDSRSGIDLPPEARRLGYVFQEHRLFPHLSVRGNLEFGQKLLPSAERTQSLDKVVELLG
IESLLDRRPAKLSGGEKQRVAIGRALLASPRILLMDEPLAALDPARKAEVLPFIAQLARR
FSVPILYVSHSMDEVLRLADTLALMDGGKVAASGPLESLMGDPGLRPLTGRYEAGAVIGA
VVSSHDSGFGISRLAFDGGTLIVGRSELPVGAKVRLRIHARDVAIAIEPPDRVSIRNVLP
AIVVSVAPADSFLVDVILACGPTRFWVQITTLAQAQLNLVPGMRVHALIKALTIARGDVA
SVD
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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