SitesBLAST
Comparing WP_308205971.1 NCBI__GCF_000058485.1:WP_308205971.1 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
45% identity, 77% coverage: 26:225/259 of query aligns to 38:239/382 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
7aheC Opua inhibited inward facing (see paper)
45% identity, 77% coverage: 26:225/259 of query aligns to 38:239/382 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
7ahdC Opua (e190q) occluded (see paper)
44% identity, 77% coverage: 26:225/259 of query aligns to 38:239/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (= T27), S61 (= S49), G62 (= G50), G64 (= G52), K65 (= K53), S66 (≠ T54), T67 (= T55), Q111 (= Q95), K161 (≠ H147), Q162 (≠ E148), S164 (= S150), G166 (= G152), M167 (≠ Q153), Q188 (≠ E174), H221 (= H207)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
41% identity, 90% coverage: 14:247/259 of query aligns to 7:240/375 of 2d62A
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)
44% identity, 88% coverage: 14:241/259 of query aligns to 4:226/393 of P9WQI3
- H193 (= H207) 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)
42% identity, 91% coverage: 8:243/259 of query aligns to 12:241/378 of P69874
- C26 (≠ R22) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (≠ Y23) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ L42) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C51) mutation to T: Loss of ATPase activity and transport.
- L60 (≠ M57) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V73) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V134) mutation to M: Loss of ATPase activity and transport.
- D172 (= D173) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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, 90% coverage: 12:243/259 of query aligns to 1:226/358 of 8y5iA
1g291 Malk (see paper)
42% identity, 85% coverage: 29:247/259 of query aligns to 18:237/372 of 1g291
- binding magnesium ion: D69 (= D82), E71 (≠ V84), K72 (≠ R85), K79 (≠ L86), D80 (≠ R87)
- binding pyrophosphate 2-: S38 (= S49), G39 (= G50), C40 (= C51), G41 (= G52), K42 (= K53), T43 (= T54), T44 (= T55)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 94% coverage: 14:257/259 of query aligns to 3:236/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y23), S38 (= S49), G39 (= G50), G41 (= G52), K42 (= K53), S43 (≠ T54), Q82 (= Q95), Q133 (≠ E148), G136 (= G151), G137 (= G152), Q138 (= Q153), H192 (= H207)
- binding magnesium ion: S43 (≠ T54), Q82 (= Q95)
8hprD Lpqy-sugabc in state 4 (see paper)
40% identity, 94% coverage: 14:257/259 of query aligns to 3:236/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y23), S38 (= S49), C40 (= C51), G41 (= G52), K42 (= K53), S43 (≠ T54), T44 (= T55), Q82 (= Q95), R129 (= R144), Q133 (≠ E148), S135 (= S150), G136 (= G151), G137 (= G152), Q159 (≠ E174), H192 (= H207)
- binding magnesium ion: S43 (≠ T54), Q82 (= Q95)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 92% coverage: 14:250/259 of query aligns to 7:229/353 of 1vciA
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 94% coverage: 14:256/259 of query aligns to 3:233/384 of 8hplC
3fvqB Crystal structure of the nucleotide binding domain fbpc complexed with atp (see paper)
43% identity, 80% coverage: 26:233/259 of query aligns to 15:222/350 of 3fvqB
- binding adenosine-5'-triphosphate: T16 (= T27), V18 (≠ A29), S38 (= S49), G39 (= G50), C40 (= C51), G41 (= G52), K42 (= K53), T43 (= T54), T44 (= T55), R133 (= R144), E137 (= E148), S139 (= S150), G141 (= G152), Q142 (= Q153)
- binding calcium ion: T43 (= T54), Q86 (= Q95)
Sites not aligning to the query:
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
39% identity, 92% coverage: 12:248/259 of query aligns to 1:234/241 of 4u00A
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, 88% coverage: 14:241/259 of query aligns to 3:224/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ Y23), S37 (= S49), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (≠ T54), T43 (= T55), Q81 (= Q95), R128 (= R144), A132 (≠ E148), S134 (= S150), G136 (= G152), Q137 (= Q153), E158 (= E174), H191 (= H207)
- binding magnesium ion: S42 (≠ T54), Q81 (= Q95)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 88% coverage: 14:241/259 of query aligns to 3:224/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ Y23), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (≠ T54), T43 (= T55), R128 (= R144), S134 (= S150), Q137 (= Q153)
- binding beryllium trifluoride ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q95), S134 (= S150), G136 (= G152), H191 (= H207)
- binding magnesium ion: S42 (≠ T54), Q81 (= Q95)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 88% coverage: 14:241/259 of query aligns to 3:224/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ Y23), V17 (= V28), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (≠ T54), T43 (= T55), R128 (= R144), A132 (≠ E148), S134 (= S150), Q137 (= Q153)
- binding tetrafluoroaluminate ion: S37 (= S49), G38 (= G50), K41 (= K53), Q81 (= Q95), S134 (= S150), G135 (= G151), G136 (= G152), E158 (= E174), H191 (= H207)
- binding magnesium ion: S42 (≠ T54), Q81 (= Q95)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 88% coverage: 14:241/259 of query aligns to 3:224/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ Y23), V17 (= V28), G38 (= G50), C39 (= C51), G40 (= G52), K41 (= K53), S42 (≠ T54), T43 (= T55), R128 (= R144), A132 (≠ E148), S134 (= S150), Q137 (= Q153)
- binding magnesium ion: S42 (≠ T54), Q81 (= Q95)
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 88% coverage: 14:241/259 of query aligns to 4:225/371 of P68187
- A85 (≠ G98) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V127) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ M130) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D132) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A139) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G152) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D173) 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)
37% identity, 85% coverage: 14:234/259 of query aligns to 3:217/374 of 2awnB
Query Sequence
>WP_308205971.1 NCBI__GCF_000058485.1:WP_308205971.1
MTTVESTTAADPMISLRGVGKRYPDGTVAVADLSLDVPAGELLCLVGPSGCGKTTTMKMI
NRLVEPTSGHILVAGEDVARTDPVRLRRRIGYVIQQIGLFPHLTVHANVGTVPRMLGWDR
ARIRARVDAMLDLVGLDPATMGRRYPHELSGGQQQRVGVARALAADPPVLLMDEPFSAID
PIARDRLQAEFLRLQREIRKTVVFVTHDLDEAIRLGDRIAVFRQGGHLEQIDPPASSAAR
PPTSSPASPVPTGRCGGCR
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