SitesBLAST
Comparing WP_068461491.1 NCBI__GCF_001541235.1:WP_068461491.1 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)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
47% identity, 85% coverage: 1:215/254 of query aligns to 2:225/658 of 8wm7C
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
47% identity, 85% coverage: 1:215/254 of query aligns to 2:225/256 of 8w9mC
- binding adenosine-5'-triphosphate: F12 (= F11), Y20 (≠ V17), S42 (= S37), G43 (= G38), G45 (= G40), K46 (= K41), S47 (= S42), T48 (= T43), Q83 (= Q78), K132 (= K123), E136 (= E127), S138 (= S129), G140 (= G131), H195 (= H186)
- binding magnesium ion: S47 (= S42), Q83 (= Q78)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
45% identity, 80% coverage: 16:217/254 of query aligns to 22:228/257 of 8wm7D
Sites not aligning to the query:
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
45% identity, 80% coverage: 16:217/254 of query aligns to 20:226/256 of 8w9mD
- binding adenosine-5'-triphosphate: H40 (≠ A36), S41 (= S37), G42 (= G38), G44 (= G40), K45 (= K41), S46 (= S42), T47 (= T43), Q82 (= Q78), Q135 (≠ E127), S137 (= S129), G139 (= G131), M140 (≠ Q132), H194 (= H186)
- binding magnesium ion: S46 (= S42), Q82 (= Q78)
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)
45% identity, 83% coverage: 1:210/254 of query aligns to 17:228/378 of P69874
- C26 (≠ A10) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F11) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (≠ S30) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C39) mutation to T: Loss of ATPase activity and transport.
- L60 (= L45) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V61) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ I115) mutation to M: Loss of ATPase activity and transport.
- D172 (= D152) 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)
44% identity, 83% coverage: 1:210/254 of query aligns to 2:213/358 of 8y5iA
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
42% identity, 80% coverage: 11:213/254 of query aligns to 13:226/375 of 2d62A
1g291 Malk (see paper)
43% identity, 77% coverage: 7:202/254 of query aligns to 9:214/372 of 1g291
- binding magnesium ion: D69 (≠ T68), E71 (≠ H70), K72 (≠ P71), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S37), G39 (= G38), C40 (= C39), G41 (= G40), K42 (= K41), T43 (≠ S42), T44 (= T43)
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)
38% identity, 94% coverage: 6:244/254 of query aligns to 11:238/353 of 1vciA
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, 83% coverage: 4:215/254 of query aligns to 6:219/393 of P9WQI3
- H193 (= H186) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
42% identity, 83% coverage: 2:211/254 of query aligns to 3:214/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
42% identity, 83% coverage: 2:211/254 of query aligns to 4:215/371 of P68187
- A85 (≠ R81) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S102) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V108) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ A111) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D113) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ V118) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G131) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D152) 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)
42% identity, 83% coverage: 2:211/254 of query aligns to 3:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F11), S37 (= S37), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), Q81 (= Q78), R128 (≠ K123), A132 (≠ E127), S134 (= S129), G136 (= G131), Q137 (= Q132), E158 (= E153), H191 (= H186)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
42% identity, 83% coverage: 2:211/254 of query aligns to 3:214/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F11), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ K123), S134 (= S129), Q137 (= Q132)
- binding beryllium trifluoride ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q78), S134 (= S129), G136 (= G131), H191 (= H186)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
42% identity, 83% coverage: 2:211/254 of query aligns to 3:214/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (= V17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ K123), A132 (≠ E127), S134 (= S129), Q137 (= Q132)
- binding tetrafluoroaluminate ion: S37 (= S37), G38 (= G38), K41 (= K41), Q81 (= Q78), S134 (= S129), G135 (= G130), G136 (= G131), E158 (= E153), H191 (= H186)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
42% identity, 83% coverage: 2:211/254 of query aligns to 3:214/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F11), V17 (= V17), G38 (= G38), C39 (= C39), G40 (= G40), K41 (= K41), S42 (= S42), T43 (= T43), R128 (≠ K123), A132 (≠ E127), S134 (= S129), Q137 (= Q132)
- binding magnesium ion: S42 (= S42), Q81 (= Q78)
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
42% identity, 83% coverage: 2:211/254 of query aligns to 1:212/367 of 1q12A
- binding adenosine-5'-triphosphate: W10 (≠ F11), S35 (= S37), G36 (= G38), C37 (= C39), G38 (= G40), K39 (= K41), S40 (= S42), T41 (= T43), R126 (≠ K123), A130 (≠ E127), S132 (= S129), G134 (= G131), Q135 (= Q132)
8hplC Lpqy-sugabc in state 1 (see paper)
41% identity, 78% coverage: 4:201/254 of query aligns to 5:205/384 of 8hplC
8hprD Lpqy-sugabc in state 4 (see paper)
41% identity, 78% coverage: 4:201/254 of query aligns to 5:207/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F11), S38 (= S37), C40 (= C39), G41 (= G40), K42 (= K41), S43 (= S42), T44 (= T43), Q82 (= Q78), R129 (≠ K123), Q133 (≠ E127), S135 (= S129), G136 (= G130), G137 (= G131), Q159 (≠ E153), H192 (= H186)
- binding magnesium ion: S43 (= S42), Q82 (= Q78)
8hprC Lpqy-sugabc in state 4 (see paper)
41% identity, 78% coverage: 4:201/254 of query aligns to 5:207/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F11), S38 (= S37), G39 (= G38), G41 (= G40), K42 (= K41), S43 (= S42), Q82 (= Q78), Q133 (≠ E127), G136 (= G130), G137 (= G131), Q138 (= Q132), H192 (= H186)
- binding magnesium ion: S43 (= S42), Q82 (= Q78)
Query Sequence
>WP_068461491.1 NCBI__GCF_001541235.1:WP_068461491.1
MLHIGHVSKAFARGGAVLADVDLTVERGESVAIVGASGCGKSTLLRIIAGLEPPSRGTVT
VAGEEIRTPHPAVGMIFQEPRLLPWLTVAENIAFGITSLPASERTARVQEALDLIGLVEH
ASKWPRELSGGQSQRVAIARALVARPSVILLDEPFSALDAVTRVDLQRHMRALGRRMHLT
LVIVTHDLEEALILGDRVAIMQPNPGRIAKIVTVPGDGDTDLALRELASSFAHLNGARNA
AILEGAHIQYAHTS
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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