SitesBLAST
Comparing WP_040574412.1 NCBI__GCF_000421465.1:WP_040574412.1 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)
8wm7D Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
40% identity, 88% coverage: 5:218/243 of query aligns to 7:234/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
39% identity, 88% coverage: 5:218/243 of query aligns to 5:232/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (≠ F12), H40 (≠ P42), S41 (= S43), G42 (= G44), G44 (= G46), K45 (= K47), S46 (≠ T48), T47 (= T49), Q82 (= Q80), Q135 (≠ R126), S137 (= S128), G139 (= G130), M140 (= M131), H194 (= H185)
- binding magnesium ion: S46 (≠ T48), Q82 (= Q80)
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
40% identity, 83% coverage: 3:204/243 of query aligns to 3:214/256 of 8w9mC
- binding adenosine-5'-triphosphate: F12 (= F12), Y20 (≠ H21), S42 (= S43), G43 (= G44), G45 (= G46), K46 (= K47), S47 (≠ T48), T48 (= T49), Q83 (= Q80), K132 (≠ T122), E136 (≠ R126), S138 (= S128), G140 (= G130), H195 (= H185)
- binding magnesium ion: S47 (≠ T48), Q83 (= Q80)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
40% identity, 83% coverage: 3:204/243 of query aligns to 3:214/658 of 8wm7C
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 74% coverage: 22:201/243 of query aligns to 20:203/353 of 1vciA
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)
40% identity, 74% coverage: 21:200/243 of query aligns to 17:208/393 of P9WQI3
- H193 (= H185) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hplC Lpqy-sugabc in state 1 (see paper)
37% identity, 76% coverage: 17:200/243 of query aligns to 10:205/384 of 8hplC
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
38% identity, 73% coverage: 23:200/243 of query aligns to 20:218/232 of 1f3oA
Sites not aligning to the query:
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
38% identity, 73% coverage: 23:200/243 of query aligns to 20:218/230 of 1l2tA
- binding adenosine-5'-triphosphate: S40 (= S43), G41 (= G44), S42 (≠ C45), G43 (= G46), K44 (= K47), S45 (≠ T48), T46 (= T49), F138 (= F119), Q145 (≠ R126), S147 (= S128), G149 (= G130), Q150 (≠ M131), H204 (= H185)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
37% identity, 73% coverage: 23:200/243 of query aligns to 18:207/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S43), C40 (= C45), G41 (= G46), K42 (= K47), S43 (≠ T48), T44 (= T49), Q82 (= Q80), R129 (≠ T122), Q133 (≠ R126), S135 (= S128), G136 (≠ L129), G137 (= G130), Q159 (≠ E152), H192 (= H185)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q80)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
37% identity, 73% coverage: 23:200/243 of query aligns to 18:207/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S43), G39 (= G44), G41 (= G46), K42 (= K47), S43 (≠ T48), Q82 (= Q80), Q133 (≠ R126), G136 (≠ L129), G137 (= G130), Q138 (≠ M131), H192 (= H185)
- binding magnesium ion: S43 (≠ T48), Q82 (= Q80)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
37% identity, 74% coverage: 22:201/243 of query aligns to 20:217/375 of 2d62A
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 72% coverage: 25:200/243 of query aligns to 19:206/374 of 2awnB
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, 72% coverage: 25:200/243 of query aligns to 20:207/371 of P68187
- A85 (≠ R83) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D103) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V107) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ L110) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E112) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A117) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G130) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D151) 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)
38% identity, 72% coverage: 25:200/243 of query aligns to 19:206/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), Q81 (= Q80), R128 (≠ T122), A132 (≠ R126), S134 (= S128), G136 (= G130), Q137 (≠ M131), E158 (= E152), H191 (= H185)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q80)
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, 72% coverage: 25:200/243 of query aligns to 19:206/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (≠ T122), S134 (= S128), Q137 (≠ M131)
- binding beryllium trifluoride ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q80), S134 (= S128), G136 (= G130), H191 (= H185)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q80)
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, 72% coverage: 25:200/243 of query aligns to 19:206/371 of 3puwA
- binding adenosine-5'-diphosphate: G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (≠ T122), A132 (≠ R126), S134 (= S128), Q137 (≠ M131)
- binding tetrafluoroaluminate ion: S37 (= S43), G38 (= G44), K41 (= K47), Q81 (= Q80), S134 (= S128), G135 (≠ L129), G136 (= G130), E158 (= E152), H191 (= H185)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q80)
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, 72% coverage: 25:200/243 of query aligns to 19:206/371 of 3puvA
- binding adenosine-5'-diphosphate: G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (≠ T48), T43 (= T49), R128 (≠ T122), A132 (≠ R126), S134 (= S128), Q137 (≠ M131)
- binding magnesium ion: S42 (≠ T48), Q81 (= Q80)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 72% coverage: 25:200/243 of query aligns to 17:204/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S43), G36 (= G44), C37 (= C45), G38 (= G46), K39 (= K47), S40 (≠ T48), T41 (= T49), R126 (≠ T122), A130 (≠ R126), S132 (= S128), G134 (= G130), Q135 (≠ M131)
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)
39% identity, 79% coverage: 9:200/243 of query aligns to 24:221/378 of P69874
- C26 (≠ V11) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F12) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F36) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C45) mutation to T: Loss of ATPase activity and transport.
- L60 (= L51) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ F67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (≠ T114) mutation to M: Loss of ATPase activity and transport.
- D172 (= D151) 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.
Query Sequence
>WP_040574412.1 NCBI__GCF_000421465.1:WP_040574412.1
MSIEIEIRRKVFPGQDRARPHTAIENLYLTLRENEFVCLVGPSGCGKTTLLNLIAGLDKD
FEGRIDFHLSQPPRLGYVFQEPRLLPWRTVRQNLELVLPSDHDPEIVTELLETTGLARFQ
HTYPSRLSLGMGRRVALARAFAVEPDILLMDEPFVSLDAAIAEKMRQLLHKLWQRRPHTI
LFVTHDLREAIALADRLVFLTPPPTRSDWEFVLPRARQVRDEHTIETLHRELRNRMQFPH
APE
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