SitesBLAST
Comparing AO353_15055 FitnessBrowser__pseudo3_N2E3:AO353_15055 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)
43% identity, 69% coverage: 49:240/278 of query aligns to 46:244/382 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
- binding phosphoaminophosphonic acid-adenylate ester: 12, 39, 40, 41
7aheC Opua inhibited inward facing (see paper)
43% identity, 69% coverage: 49:240/278 of query aligns to 46:244/382 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)
43% identity, 69% coverage: 48:240/278 of query aligns to 45:244/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S64), G62 (= G65), G64 (= G67), K65 (= K68), S66 (= S69), T67 (≠ S70), Q111 (= Q105), K161 (= K155), Q162 (= Q156), S164 (= S158), G166 (= G160), M167 (= M161), Q188 (≠ E182), H221 (= H215)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 77% coverage: 27:240/278 of query aligns to 5:215/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (= Y34), S38 (= S64), G39 (= G65), G41 (= G67), K42 (= K68), S43 (= S69), Q82 (= Q105), Q133 (= Q156), G136 (= G159), G137 (= G160), Q138 (≠ M161), H192 (= H215)
- binding magnesium ion: S43 (= S69), Q82 (= Q105)
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 77% coverage: 27:240/278 of query aligns to 5:215/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (= Y34), S38 (= S64), C40 (= C66), G41 (= G67), K42 (= K68), S43 (= S69), T44 (≠ S70), Q82 (= Q105), R129 (≠ N152), Q133 (= Q156), S135 (= S158), G136 (= G159), G137 (= G160), Q159 (≠ E182), H192 (= H215)
- binding magnesium ion: S43 (= S69), Q82 (= Q105)
8hplC Lpqy-sugabc in state 1 (see paper)
42% identity, 77% coverage: 27:240/278 of query aligns to 5:213/384 of 8hplC
1g291 Malk (see paper)
44% identity, 69% coverage: 40:230/278 of query aligns to 14:213/372 of 1g291
- binding magnesium ion: D69 (≠ G95), E71 (vs. gap), K72 (vs. gap), K79 (vs. gap), D80 (≠ G97)
- binding pyrophosphate 2-: S38 (= S64), G39 (= G65), C40 (= C66), G41 (= G67), K42 (= K68), T43 (≠ S69), T44 (≠ S70)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
41% identity, 72% coverage: 40:240/278 of query aligns to 17:224/375 of 2d62A
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, 81% coverage: 27:251/278 of query aligns to 6:229/393 of P9WQI3
- H193 (= H215) 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)
40% identity, 72% coverage: 40:240/278 of query aligns to 13:214/374 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)
40% identity, 72% coverage: 40:240/278 of query aligns to 14:215/371 of P68187
- A85 (≠ T108) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R133) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V141) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V144) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (vs. gap) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T147) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G160) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D181) 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)
40% identity, 72% coverage: 40:240/278 of query aligns to 13:214/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S64), G38 (= G65), C39 (= C66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (≠ S70), Q81 (= Q105), R128 (≠ N152), A132 (≠ Q156), S134 (= S158), G136 (= G160), Q137 (≠ M161), E158 (= E182), H191 (= H215)
- binding magnesium ion: S42 (= S69), Q81 (= Q105)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
40% identity, 72% coverage: 40:240/278 of query aligns to 13:214/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G65), C39 (= C66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (≠ S70), R128 (≠ N152), S134 (= S158), Q137 (≠ M161)
- binding beryllium trifluoride ion: S37 (= S64), G38 (= G65), K41 (= K68), Q81 (= Q105), S134 (= S158), G136 (= G160), H191 (= H215)
- binding magnesium ion: S42 (= S69), Q81 (= Q105)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
40% identity, 72% coverage: 40:240/278 of query aligns to 13:214/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ A44), G38 (= G65), C39 (= C66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (≠ S70), R128 (≠ N152), A132 (≠ Q156), S134 (= S158), Q137 (≠ M161)
- binding tetrafluoroaluminate ion: S37 (= S64), G38 (= G65), K41 (= K68), Q81 (= Q105), S134 (= S158), G135 (= G159), G136 (= G160), E158 (= E182), H191 (= H215)
- binding magnesium ion: S42 (= S69), Q81 (= Q105)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
40% identity, 72% coverage: 40:240/278 of query aligns to 13:214/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ A44), G38 (= G65), C39 (= C66), G40 (= G67), K41 (= K68), S42 (= S69), T43 (≠ S70), R128 (≠ N152), A132 (≠ Q156), S134 (= S158), Q137 (≠ M161)
- binding magnesium ion: S42 (= S69), Q81 (= Q105)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
40% identity, 72% coverage: 40:240/278 of query aligns to 11:212/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S64), G36 (= G65), C37 (= C66), G38 (= G67), K39 (= K68), S40 (= S69), T41 (≠ S70), R126 (≠ N152), A130 (≠ Q156), S132 (= S158), G134 (= G160), Q135 (≠ M161)
Sites not aligning to the query:
P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
40% identity, 76% coverage: 29:240/278 of query aligns to 3:215/369 of P19566
- L86 (= L109) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P183) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D188) 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.
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 69% coverage: 47:239/278 of query aligns to 35:228/378 of P69874
- F45 (= F57) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C66) mutation to T: Loss of ATPase activity and transport.
- L60 (= L72) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (≠ V88) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V144) mutation to M: Loss of ATPase activity and transport.
- D172 (= D181) 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.
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
41% identity, 72% coverage: 40:240/278 of query aligns to 17:210/353 of 1vciA
Sites not aligning to the query:
2awnC Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
39% identity, 71% coverage: 43:240/278 of query aligns to 9:184/344 of 2awnC
Query Sequence
>AO353_15055 FitnessBrowser__pseudo3_N2E3:AO353_15055
MGSVTAANHRFTTPTAALVHAAPRLQVDKVSLRYQKPDGGMFTALEKVSFEVPDQQFAVL
VGPSGCGKSSLLYLTAGLAEPTEGEIYVGGQHVEGPGADRGMVFQSYTLFPWLTVRQNVE
FGLKRRGMPAAQRKEIVDYYVNEVGLTGFADNYAKQLSGGMMQRVAIARALANDPQILLM
DEPFGALDSQTRLQMQQLLLRVWGNSKKTVLFVTHDIDEAILLGDRVYVMGARPGRIKQI
LDVPIERPRTLDMVMERSFIEMKREIFGLLHDELEEAH
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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