SitesBLAST
Comparing Synpcc7942_2105 FitnessBrowser__SynE:Synpcc7942_2105 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)
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, 71% coverage: 33:238/289 of query aligns to 5:211/393 of P9WQI3
- H193 (= H220) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 71% coverage: 33:238/289 of query aligns to 4:210/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ S41), S38 (= S67), G39 (= G68), G41 (= G70), K42 (= K71), S43 (= S72), Q82 (= Q108), Q133 (= Q161), G136 (= G164), G137 (= G165), Q138 (≠ M166), H192 (= H220)
- binding magnesium ion: S43 (= S72), Q82 (= Q108)
8hprD Lpqy-sugabc in state 4 (see paper)
40% identity, 71% coverage: 33:238/289 of query aligns to 4:210/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ S41), S38 (= S67), C40 (= C69), G41 (= G70), K42 (= K71), S43 (= S72), T44 (= T73), Q82 (= Q108), R129 (= R157), Q133 (= Q161), S135 (= S163), G136 (= G164), G137 (= G165), Q159 (≠ E187), H192 (= H220)
- binding magnesium ion: S43 (= S72), Q82 (= Q108)
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 71% coverage: 33:238/289 of query aligns to 4:208/384 of 8hplC
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 69% coverage: 51:250/289 of query aligns to 36:239/378 of P69874
- F45 (= F60) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C69) mutation to T: Loss of ATPase activity and transport.
- L60 (= L75) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L91) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V149) mutation to M: Loss of ATPase activity and transport.
- D172 (= D186) 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.
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 66% coverage: 47:238/289 of query aligns to 21:219/375 of 2d62A
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
36% identity, 77% coverage: 16:238/289 of query aligns to 2:239/382 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)
36% identity, 77% coverage: 16:238/289 of query aligns to 2:239/382 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)
35% identity, 81% coverage: 19:251/289 of query aligns to 5:255/260 of 7ahdC
- binding adenosine-5'-triphosphate: F12 (= F26), T39 (≠ Y45), S61 (= S67), G62 (= G68), G64 (= G70), K65 (= K71), S66 (= S72), T67 (= T73), Q111 (= Q108), K161 (≠ G160), Q162 (= Q161), S164 (= S163), G166 (= G165), M167 (= M166), Q188 (≠ E187), H221 (= H220)
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
39% identity, 67% coverage: 45:238/289 of query aligns to 19:205/353 of 1vciA
Sites not aligning to the query:
1g291 Malk (see paper)
36% identity, 71% coverage: 47:251/289 of query aligns to 18:232/372 of 1g291
- binding magnesium ion: D69 (≠ S98), E71 (≠ G100), K72 (≠ P101), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S67), G39 (= G68), C40 (= C69), G41 (= G70), K42 (= K71), T43 (≠ S72), T44 (= T73)
Sites not aligning to the query:
3d31A Modbc from methanosarcina acetivorans (see paper)
39% identity, 67% coverage: 44:238/289 of query aligns to 12:204/348 of 3d31A
Sites not aligning to the query:
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
41% identity, 66% coverage: 47:238/289 of query aligns to 20:221/232 of 1f3oA
Sites not aligning to the query:
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
38% identity, 71% coverage: 46:249/289 of query aligns to 16:220/374 of 2awnB
Sites not aligning to the query:
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
40% identity, 66% coverage: 47:238/289 of query aligns to 20:221/230 of 1l2tA
- binding adenosine-5'-triphosphate: S40 (= S67), G41 (= G68), S42 (≠ C69), G43 (= G70), K44 (= K71), S45 (= S72), T46 (= T73), F138 (≠ A154), Q145 (= Q161), S147 (= S163), G149 (= G165), Q150 (≠ M166), H204 (= H220)
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)
38% identity, 71% coverage: 46:249/289 of query aligns to 16:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S67), G38 (= G68), C39 (= C69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), Q81 (= Q108), R128 (= R157), A132 (≠ Q161), S134 (= S163), G136 (= G165), Q137 (≠ M166), E158 (= E187), H191 (= H220)
- binding magnesium ion: S42 (= S72), Q81 (= Q108)
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, 71% coverage: 46:249/289 of query aligns to 16:220/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G68), C39 (= C69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (= R157), S134 (= S163), Q137 (≠ M166)
- binding beryllium trifluoride ion: S37 (= S67), G38 (= G68), K41 (= K71), Q81 (= Q108), S134 (= S163), G136 (= G165), H191 (= H220)
- binding magnesium ion: S42 (= S72), Q81 (= Q108)
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, 71% coverage: 46:249/289 of query aligns to 16:220/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ A47), G38 (= G68), C39 (= C69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (= R157), A132 (≠ Q161), S134 (= S163), Q137 (≠ M166)
- binding tetrafluoroaluminate ion: S37 (= S67), G38 (= G68), K41 (= K71), Q81 (= Q108), S134 (= S163), G135 (= G164), G136 (= G165), E158 (= E187), H191 (= H220)
- binding magnesium ion: S42 (= S72), Q81 (= Q108)
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, 71% coverage: 46:249/289 of query aligns to 16:220/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ A47), G38 (= G68), C39 (= C69), G40 (= G70), K41 (= K71), S42 (= S72), T43 (= T73), R128 (= R157), A132 (≠ Q161), S134 (= S163), Q137 (≠ M166)
- binding magnesium ion: S42 (= S72), Q81 (= Q108)
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, 71% coverage: 46:249/289 of query aligns to 17:221/371 of P68187
- A85 (= A111) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ R130) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ A138) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (= V141) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E147) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T152) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G165) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D186) 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.
Query Sequence
>Synpcc7942_2105 FitnessBrowser__SynE:Synpcc7942_2105
MISEAVPAKEETGQAQLLIEQVGKVFTVNSPSLLDRLRQRSPKRYVALEDVNLTIASNTF
VSIIGPSGCGKSTLLNLIAGLDLPTSGQILLDGQRIRSPGPDRGIVFQNYALMPWMTALE
NVIFAVETARPNLSKSQAREVAREHLELVGLTKAADRYPGQISGGMKQRVAIARALSIRP
KLLLMDEPFGALDALTRGYLQEEVLRIWEANKLSVVLITHSIDEALLLSDRIVVMSRGPR
ATIREVIDLPAVRPRQRSVIEEDERFVKIKLRLEEHLFNETRAVEEASV
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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