SitesBLAST
Comparing WP_109967750.1 NCBI__GCF_003173355.1:WP_109967750.1 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)
47% identity, 100% coverage: 1:214/214 of query aligns to 1:213/348 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)
40% identity, 87% coverage: 21:207/214 of query aligns to 38:226/378 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 (≠ Q59) 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)
39% identity, 87% coverage: 21:207/214 of query aligns to 23:211/358 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)
41% identity, 90% coverage: 20:211/214 of query aligns to 24:216/393 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.
1g291 Malk (see paper)
38% identity, 90% coverage: 20:211/214 of query aligns to 23:221/372 of 1g291
- binding magnesium ion: D69 (≠ N60), E71 (≠ M62), K72 (≠ D63), K79 (≠ E70), D80 (≠ K71)
- binding pyrophosphate 2-: S38 (= S35), G39 (= G36), C40 (≠ S37), G41 (= G38), K42 (= K39), T43 (= T40), T44 (≠ L41)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
38% identity, 86% coverage: 20:204/214 of query aligns to 26:217/375 of 2d62A
8hplC Lpqy-sugabc in state 1 (see paper)
38% identity, 88% coverage: 20:207/214 of query aligns to 21:210/384 of 8hplC
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
38% identity, 88% coverage: 20:207/214 of query aligns to 23:212/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S35), G39 (= G36), G41 (= G38), K42 (= K39), S43 (≠ T40), Q82 (= Q79), Q133 (≠ T128), G136 (= G131), G137 (= G132), Q138 (≠ E133), H192 (= H187)
- binding magnesium ion: S43 (≠ T40), Q82 (= Q79)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
38% identity, 88% coverage: 20:207/214 of query aligns to 23:212/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S35), C40 (≠ S37), G41 (= G38), K42 (= K39), S43 (≠ T40), T44 (≠ L41), Q82 (= Q79), R129 (= R124), Q133 (≠ T128), S135 (= S130), G136 (= G131), G137 (= G132), Q159 (≠ E154), H192 (= H187)
- binding magnesium ion: S43 (≠ T40), Q82 (= Q79)
Sites not aligning to the query:
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
37% identity, 97% coverage: 2:209/214 of query aligns to 7:209/353 of 1vciA
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 97% coverage: 6:212/214 of query aligns to 22:216/374 of 2awnB
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)
37% identity, 88% coverage: 25:212/214 of query aligns to 28:217/369 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.
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 97% coverage: 6:212/214 of query aligns to 23:217/371 of P68187
- A85 (≠ S82) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R101) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ I112) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 97% coverage: 6:212/214 of query aligns to 20:214/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S35), G36 (= G36), C37 (≠ S37), G38 (= G38), K39 (= K39), S40 (≠ T40), T41 (≠ L41), R126 (= R124), A130 (≠ T128), S132 (= S130), G134 (= G132), Q135 (≠ E133)
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)
36% identity, 97% coverage: 6:212/214 of query aligns to 22:216/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S35), G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ L41), Q81 (= Q79), R128 (= R124), A132 (≠ T128), 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)
36% identity, 97% coverage: 6:212/214 of query aligns to 22:216/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ L41), 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)
36% identity, 97% coverage: 6:212/214 of query aligns to 22:216/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ L41), R128 (= R124), A132 (≠ T128), 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)
36% identity, 97% coverage: 6:212/214 of query aligns to 22:216/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G36), C39 (≠ S37), G40 (= G38), K41 (= K39), S42 (≠ T40), T43 (≠ L41), R128 (= R124), A132 (≠ T128), S134 (= S130), Q137 (≠ E133)
- binding magnesium ion: S42 (≠ T40), Q81 (= Q79)
Sites not aligning to the query:
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
36% identity, 87% coverage: 29:214/214 of query aligns to 31:221/241 of 4u00A
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
33% identity, 98% coverage: 1:209/214 of query aligns to 1:216/240 of 4ymuJ
- binding adenosine-5'-triphosphate: F11 (≠ A11), V16 (= V17), S36 (= S35), G37 (= G36), S38 (= S37), G39 (= G38), K40 (= K39), S41 (≠ T40), T42 (≠ L41), E162 (= E154), H194 (= H187)
- binding magnesium ion: S41 (≠ T40), E162 (= E154)
Query Sequence
>WP_109967750.1 NCBI__GCF_003173355.1:WP_109967750.1
MIAISNLVVHAGQFELVIDSFTLPDDAWCIISGPSGSGKTLFLETIAGFYQPCSGKIIQN
GMDITYFSPEKRGIGIVFQDYSLFPHMTVAKNIGYGLAIRRHSDIHNIVLDISRKLGIDS
LLDRNPLTLSGGEKQRVAIARALVVKPKLLLLDEPASALDLQAKKELWDDIRDLFEQGGL
TIIHVTHDISESNNLGTHKILLMNGKIVKTIKHE
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