SitesBLAST
Comparing AO356_00615 FitnessBrowser__pseudo5_N2C3_1:AO356_00615 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)
44% identity, 94% coverage: 4:387/407 of query aligns to 3:380/382 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 (≠ K280), S297 (≠ Q302), S298 (≠ N303)
- binding phosphoaminophosphonic acid-adenylate ester: F12 (= F13), T39 (≠ I40), V40 (= V41), G41 (= G42), G62 (= G63), G64 (= G65), K65 (= K66), D187 (= D192), E188 (= E193)
7aheC Opua inhibited inward facing (see paper)
44% identity, 94% coverage: 4:387/407 of query aligns to 3:380/382 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 (≠ K280), S297 (≠ Q302), S298 (≠ N303)
7ahdC Opua (e190q) occluded (see paper)
53% identity, 64% coverage: 4:265/407 of query aligns to 3:260/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F13), T39 (≠ I40), S61 (= S62), G62 (= G63), G64 (= G65), K65 (= K66), S66 (= S67), T67 (≠ S68), Q111 (= Q116), K161 (≠ D166), Q162 (≠ E167), S164 (= S169), G166 (= G171), M167 (= M172), Q188 (≠ E193), H221 (= H226)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 69% coverage: 33:311/407 of query aligns to 12:281/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 58% coverage: 47:282/407 of query aligns to 37:262/378 of P69874
- F45 (≠ I55) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (≠ S64) mutation to T: Loss of ATPase activity and transport.
- L60 (= L70) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V86) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V155) mutation to M: Loss of ATPase activity and transport.
- D172 (= D192) 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)
40% identity, 59% coverage: 38:279/407 of query aligns to 14:250/372 of 1g291
- binding magnesium ion: D69 (≠ S97), E71 (≠ T99), K72 (≠ P100), K79 (≠ R107), D80 (≠ T108)
- binding pyrophosphate 2-: S38 (= S62), G39 (= G63), C40 (≠ S64), G41 (= G65), K42 (= K66), T43 (≠ S67), T44 (≠ S68)
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 67% coverage: 38:308/407 of query aligns to 13:269/374 of 2awnB
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)
36% identity, 67% coverage: 38:308/407 of query aligns to 13:269/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S62), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), Q81 (= Q116), R128 (≠ K163), A132 (≠ E167), S134 (= S169), G136 (= G171), Q137 (≠ M172), E158 (= E193), H191 (= H226)
- binding magnesium ion: S42 (= S67), Q81 (= Q116)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 67% coverage: 38:308/407 of query aligns to 13:269/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), R128 (≠ K163), S134 (= S169), Q137 (≠ M172)
- binding beryllium trifluoride ion: S37 (= S62), G38 (= G63), K41 (= K66), Q81 (= Q116), S134 (= S169), G136 (= G171), H191 (= H226)
- binding magnesium ion: S42 (= S67), Q81 (= Q116)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 67% coverage: 38:308/407 of query aligns to 13:269/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ G42), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), R128 (≠ K163), A132 (≠ E167), S134 (= S169), Q137 (≠ M172)
- binding tetrafluoroaluminate ion: S37 (= S62), G38 (= G63), K41 (= K66), Q81 (= Q116), S134 (= S169), G135 (= G170), G136 (= G171), E158 (= E193), H191 (= H226)
- binding magnesium ion: S42 (= S67), Q81 (= Q116)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 67% coverage: 38:308/407 of query aligns to 13:269/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ G42), G38 (= G63), C39 (≠ S64), G40 (= G65), K41 (= K66), S42 (= S67), T43 (≠ S68), R128 (≠ K163), A132 (≠ E167), S134 (= S169), Q137 (≠ M172)
- binding magnesium ion: S42 (= S67), Q81 (= Q116)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 67% coverage: 38:308/407 of query aligns to 11:267/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S62), G36 (= G63), C37 (≠ S64), G38 (= G65), K39 (= K66), S40 (= S67), T41 (≠ S68), R126 (≠ K163), A130 (≠ E167), S132 (= S169), G134 (= G171), Q135 (≠ M172)
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)
36% identity, 67% coverage: 38:308/407 of query aligns to 14:270/371 of P68187
- A85 (= A119) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ S140) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V148) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ K151) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E153) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T158) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G171) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D192) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (≠ D262) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- F241 (≠ V276) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- W267 (= W305) mutation to G: Normal maltose transport but constitutive mal gene expression.
Sites not aligning to the query:
- 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)
36% identity, 67% coverage: 38:308/407 of query aligns to 14:268/369 of P19566
- L86 (= L120) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P194) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D199) 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.
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)
37% identity, 62% coverage: 42:292/407 of query aligns to 19:262/393 of P9WQI3
- H193 (= H226) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
38% identity, 55% coverage: 48:269/407 of query aligns to 22:237/240 of 4ymuJ
Sites not aligning to the query:
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 59% coverage: 36:274/407 of query aligns to 14:247/353 of 1oxvD
Sites not aligning to the query:
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 59% coverage: 36:274/407 of query aligns to 14:247/353 of 1oxvA
Sites not aligning to the query:
1oxuA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
36% identity, 59% coverage: 36:274/407 of query aligns to 14:247/353 of 1oxuA
Sites not aligning to the query:
Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
36% identity, 59% coverage: 36:274/407 of query aligns to 14:247/353 of Q97UY8
- S142 (= S169) mutation to A: Decrease in ATPase activity. Can form dimers.
- G144 (= G171) mutation to A: Loss of ATPase activity. Cannot form dimers. Forms an active heterodimer; when associated with A-166.
- E166 (= E193) mutation to A: Loss of ATPase activity. Can form dimers in the presence of ATP-Mg(2+). Forms an active heterodimer; when associated with A-144.; mutation to Q: Strong decrease in ATPase activity. Can form dimers in the presence of ATP alone, without Mg(2+).
Query Sequence
>AO356_00615 FitnessBrowser__pseudo5_N2C3_1:AO356_00615
MSIIRFEDVDVIFAARPKPALELLDQGFSRPEILQKTGLIVGVEKANLEINKGEICVLMG
LSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCTPAELKMMRTQRIAMVFQKFAL
MPWLTVRENISFGLEMQGRSEKECRKLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLAR
ALAMDADILLMDEPFSALDPLIRQGLQDELLDLQRKLHKTIVFVSHDLDEALKLGTRIAI
MKDGKIIQYSTPEEIVLNPADDYVRNFVAHTNPLNVLCAKSLMTPLDQCVLARDEYCLDT
AQNLWMVVNPQRHLTSVRKGATTAHVQSWNPTERIDTLARQPTCVPPITTMRDALQIRYE
TGHPLIVRDEADTVLGILGDGELYRALLGHNLSHPVLAEPARASSVA
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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