SitesBLAST
Comparing WP_022669727.1 NCBI__GCF_000420385.1:WP_022669727.1 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)
37% identity, 50% coverage: 6:215/424 of query aligns to 7:216/257 of 8wm7D
8w9mD Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
37% identity, 50% coverage: 6:215/424 of query aligns to 5:214/256 of 8w9mD
- binding adenosine-5'-triphosphate: Y12 (≠ F13), H40 (≠ P42), S41 (= S43), G42 (= G44), G44 (= G46), K45 (= K47), S46 (= S48), T47 (= T49), Q82 (= Q84), Q135 (≠ S133), S137 (= S135), G139 (= G137), M140 (= M138), H194 (= H195)
- binding magnesium ion: S46 (= S48), Q82 (= Q84)
8w9mC Cryo-em structure of the cyanobacterial nitrate transporter nrtbcd in complex with atp (see paper)
37% identity, 54% coverage: 4:231/424 of query aligns to 3:232/256 of 8w9mC
- binding adenosine-5'-triphosphate: F12 (= F13), Y20 (≠ L21), S42 (= S43), G43 (= G44), G45 (= G46), K46 (= K47), S47 (= S48), T48 (= T49), Q83 (= Q84), K132 (≠ V129), E136 (≠ S133), S138 (= S135), G140 (= G137), H195 (= H195)
- binding magnesium ion: S47 (= S48), Q83 (= Q84)
8wm7C Cryo-em structure of cyanobacterial nitrate/nitrite transporter nrtbcd in complex with signalling protein pii (see paper)
38% identity, 54% coverage: 4:231/424 of query aligns to 3:232/658 of 8wm7C
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
40% identity, 49% coverage: 4:210/424 of query aligns to 3:236/382 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
7aheC Opua inhibited inward facing (see paper)
40% identity, 49% coverage: 4:210/424 of query aligns to 3:236/382 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)
39% identity, 49% coverage: 4:210/424 of query aligns to 3:236/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F13), T39 (vs. gap), S61 (= S43), G62 (= G44), G64 (= G46), K65 (= K47), S66 (= S48), T67 (= T49), Q111 (= Q84), K161 (= K132), Q162 (≠ S133), S164 (= S135), G166 (= G137), M167 (= M138), Q188 (≠ E159), H221 (= H195)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
36% identity, 49% coverage: 3:210/424 of query aligns to 1:216/375 of 2d62A
1g291 Malk (see paper)
37% identity, 45% coverage: 21:210/424 of query aligns to 16:213/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (≠ Q72), K72 (≠ S73), K79 (vs. gap), D80 (≠ N76)
- binding pyrophosphate 2-: S38 (= S43), G39 (= G44), C40 (= C45), G41 (= G46), K42 (= K47), T43 (≠ S48), T44 (= T49)
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, 46% coverage: 23:218/424 of query aligns to 32:227/378 of P69874
- F45 (≠ I36) 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 (≠ Y67) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V121) mutation to M: Loss of ATPase activity and transport.
- D172 (= D158) 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.
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
34% identity, 56% coverage: 3:238/424 of query aligns to 1:242/343 of P30750
- 40:46 (vs. 43:49, 86% identical) binding ATP
- E166 (= E159) mutation to Q: Exhibits little ATPase activity.
Sites not aligning to the query:
- 278:283 binding L-methionine
- 295 N→A: Reduces the binding of L-methionine to undetectable levels.
- 295:296 binding L-methionine
3d31A Modbc from methanosarcina acetivorans (see paper)
40% identity, 44% coverage: 24:210/424 of query aligns to 16:201/348 of 3d31A
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
41% identity, 45% coverage: 20:210/424 of query aligns to 13:209/240 of 4ymuJ
- binding adenosine-5'-triphosphate: V16 (= V23), S36 (= S43), G37 (= G44), S38 (≠ C45), G39 (= G46), K40 (= K47), S41 (= S48), T42 (= T49), E162 (= E159), H194 (= H195)
- binding magnesium ion: S41 (= S48), E162 (= E159)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
34% identity, 56% coverage: 2:238/424 of query aligns to 1:243/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
34% identity, 56% coverage: 2:238/424 of query aligns to 1:243/344 of 3tuiC
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
34% identity, 56% coverage: 2:238/424 of query aligns to 1:243/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: F12 (= F13), Q14 (≠ S16), I19 (≠ L21), S41 (= S43), G42 (= G44), A43 (≠ C45), G44 (= G46), K45 (= K47), S46 (= S48), T47 (= T49), N141 (≠ S133), S143 (= S135), Q146 (≠ M138), H200 (= H195)
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
40% identity, 46% coverage: 23:218/424 of query aligns to 17:212/358 of 8y5iA
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)
35% identity, 56% coverage: 1:237/424 of query aligns to 1:234/371 of P68187
- A85 (= A87) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ N104) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I114) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V117) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D119) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ E124) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G137) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D158) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ Q231) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
Sites not aligning to the query:
- 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)
35% identity, 55% coverage: 4:237/424 of query aligns to 3:233/374 of 2awnB
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
35% identity, 55% coverage: 4:237/424 of query aligns to 3:233/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F13), S37 (= S43), G38 (= G44), C39 (= C45), G40 (= G46), K41 (= K47), S42 (= S48), T43 (= T49), Q81 (= Q84), R128 (≠ V129), A132 (≠ S133), S134 (= S135), G136 (= G137), Q137 (≠ M138), E158 (= E159), H191 (= H195)
- binding magnesium ion: S42 (= S48), Q81 (= Q84)
Query Sequence
>WP_022669727.1 NCBI__GCF_000420385.1:WP_022669727.1
MEIIKLENINMIFPISKSESLTVLENISLSIEEGKIVSILGPSGCGKSTLLRIITGLLKP
TKGKVFYKGKVQSGVNDKMAMVFQNFALFPWKTVWDNIAIGIRNREIRNKDEMIKRVIDI
VGLEGFEDVYPKSLSGGMKQRVGIARALVSNPEILCMDEPFSALDVLTAENLREELMDLW
LSRKTSLKGIVIVTHNITEAVYMSDEIIIMASRPGRVQLVYKNKLSYPRDQNSADFLKIV
DAIRNYLTKNIIPDEPYTKIHEQLLPIPNATVGEVIGLLEVLEDNDGKIEMFELSERINR
RFTVAMIIATAAELMGFVQTPFRYIVLTNTGRKFLDADINERKEIFRTELLKLPIVKIFV
KFIKENNGSINSKEAKKFLRKKLPKEKPNSVLKPLLNFCMYAEILDYDSRDDEISINPDI
PIKI
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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