SitesBLAST
Comparing WP_073040418.1 NCBI__GCF_900129305.1:WP_073040418.1 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)
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
46% identity, 98% coverage: 6:396/401 of query aligns to 1:381/382 of 7ahhC
- 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: L275 (≠ I291), S297 (≠ E311), S298 (≠ C312)
- binding phosphoaminophosphonic acid-adenylate ester: F12 (= F17), T39 (= T45), V40 (= V46), G41 (≠ A47), G62 (= G68), G64 (= G70), K65 (= K71), D187 (= D193), E188 (= E194)
7aheC Opua inhibited inward facing (see paper)
46% identity, 98% coverage: 6:396/401 of query aligns to 1:381/382 of 7aheC
- 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: L275 (≠ I291), S297 (≠ E311), S298 (≠ C312)
7ahdC Opua (e190q) occluded (see paper)
57% identity, 65% coverage: 6:266/401 of query aligns to 1:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F17), T39 (= T45), S61 (= S67), G62 (= G68), G64 (= G70), K65 (= K71), S66 (= S72), T67 (= T73), Q111 (= Q117), K161 (≠ A167), Q162 (≠ E168), S164 (= S170), G166 (= G172), M167 (= M173), Q188 (≠ E194), H221 (= H227)
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
37% identity, 67% coverage: 4:271/401 of query aligns to 3:245/375 of 2d62A
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
41% identity, 56% coverage: 47:269/401 of query aligns to 20:241/343 of P30750
- 40:46 (vs. 67:73, 86% identical) binding ATP
- E166 (= E194) 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
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
41% identity, 56% coverage: 47:269/401 of query aligns to 21:242/344 of 6cvlD
- binding phosphothiophosphoric acid-adenylate ester: S41 (= S67), G42 (= G68), A43 (≠ S69), G44 (= G70), K45 (= K71), S46 (= S72), T47 (= T73), N141 (≠ E168), S143 (= S170), Q146 (≠ M173), H200 (= H227)
Sites not aligning to the query:
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
41% identity, 56% coverage: 47:269/401 of query aligns to 21:242/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
41% identity, 56% coverage: 47:269/401 of query aligns to 21:242/344 of 3tuiC
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)
41% identity, 56% coverage: 51:273/401 of query aligns to 36:252/378 of P69874
- F45 (≠ I60) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S69) mutation to T: Loss of ATPase activity and transport.
- L60 (= L75) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ I91) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V156) mutation to M: Loss of ATPase activity and transport.
- D172 (= D193) 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.
1g291 Malk (see paper)
36% identity, 68% coverage: 1:271/401 of query aligns to 1:242/372 of 1g291
- binding magnesium ion: D69 (≠ A98), E71 (≠ T100), K72 (≠ P101), K79 (≠ R108), D80 (≠ Q109)
- binding pyrophosphate 2-: S38 (= S67), G39 (= G68), C40 (≠ S69), G41 (= G70), K42 (= K71), T43 (≠ S72), T44 (= T73)
Sites not aligning to the query:
8y5iA Cryo-em structure of e.Coli spermidine transporter potd-potabc in translocation intermidiate state (see paper)
40% identity, 56% coverage: 51:273/401 of query aligns to 21:237/358 of 8y5iA
Sites not aligning to the query:
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
40% identity, 57% coverage: 43:272/401 of query aligns to 12:239/240 of 4ymuJ
- binding adenosine-5'-triphosphate: V16 (≠ A47), S36 (= S67), G37 (= G68), S38 (= S69), G39 (= G70), K40 (= K71), S41 (= S72), T42 (= T73), E162 (= E194), H194 (= H227)
- binding magnesium ion: S41 (= S72), E162 (= E194)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 57% coverage: 43:271/401 of query aligns to 13:235/374 of 2awnB
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
39% identity, 57% coverage: 43:271/401 of query aligns to 11:233/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S67), G36 (= G68), C37 (≠ S69), G38 (= G70), K39 (= K71), S40 (= S72), T41 (= T73), R126 (≠ Y164), A130 (≠ E168), S132 (= S170), G134 (= G172), Q135 (≠ M173)
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)
39% identity, 57% coverage: 43:271/401 of query aligns to 13:235/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S67), G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), Q81 (= Q117), R128 (≠ Y164), A132 (≠ E168), S134 (= S170), G136 (= G172), Q137 (≠ M173), E158 (= E194), H191 (= H227)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 57% coverage: 43:271/401 of query aligns to 13:235/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (≠ Y164), S134 (= S170), Q137 (≠ M173)
- binding beryllium trifluoride ion: S37 (= S67), G38 (= G68), K41 (= K71), Q81 (= Q117), S134 (= S170), G136 (= G172), H191 (= H227)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 57% coverage: 43:271/401 of query aligns to 13:235/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ A47), G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (≠ Y164), A132 (≠ E168), S134 (= S170), Q137 (≠ M173)
- binding tetrafluoroaluminate ion: S37 (= S67), G38 (= G68), K41 (= K71), Q81 (= Q117), S134 (= S170), G135 (= G171), G136 (= G172), E158 (= E194), H191 (= H227)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 57% coverage: 43:271/401 of query aligns to 13:235/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ A47), G38 (= G68), C39 (≠ S69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (≠ Y164), A132 (≠ E168), S134 (= S170), Q137 (≠ M173)
- binding magnesium ion: S42 (= S72), Q81 (= Q117)
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)
39% identity, 57% coverage: 43:271/401 of query aligns to 14:236/371 of P68187
- A85 (= A120) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ G141) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A149) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V152) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D154) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (= A159) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G172) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D193) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D263) 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.
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, 57% coverage: 43:271/401 of query aligns to 14:236/369 of P19566
- L86 (= L121) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (≠ A195) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D200) 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.
Query Sequence
>WP_073040418.1 NCBI__GCF_900129305.1:WP_073040418.1
MAGGGVKIQVRNLWKIFGNLSGEAAERLASDPEAALEDLSLNGCTVAVRAVDFHVNEGEI
FVIMGLSGSGKSTLLRCLNGIIEPTCGEVLIDGEGVGAMTPKRLRALRQQKMAMVFQHFA
LLPYRSVLDNVAFGLELQGVGKKERRRRAREVLDLVGLADWERYLPAELSGGMQQRVGLA
RALAVDPEILLMDEAFSALDPLIRRQMQDEFLKLVEIVKKTIVFITHDLDEALRLADRIA
VMKEGRIVQIGTPEQIVMDPADDYVEEFVGAVSRTRVIAARNIMAEPRPWISPQDRDPRE
LLRHMDRHNLECVFVTDAARRLVGVLTREELAGQGRPPRDAEPPARSVRVPAVPPDAPLS
EVVERAAATSKPIPVLDESGRILGVISRSRLLRELSHGLKA
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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