SitesBLAST
Comparing Synpcc7942_1236 FitnessBrowser__SynE:Synpcc7942_1236 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)
35% identity, 76% coverage: 31:237/274 of query aligns to 37:250/382 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
7aheC Opua inhibited inward facing (see paper)
35% identity, 76% coverage: 31:237/274 of query aligns to 37:250/382 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
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)
36% identity, 82% coverage: 19:242/274 of query aligns to 6:226/393 of P9WQI3
- H193 (= H208) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
7ahdC Opua (e190q) occluded (see paper)
34% identity, 76% coverage: 31:237/274 of query aligns to 37:250/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ Y33), S61 (= S55), G62 (= G56), G64 (= G58), K65 (= K59), S66 (= S60), T67 (= T61), Q111 (= Q96), K161 (≠ D148), Q162 (= Q149), S164 (= S151), G166 (= G153), M167 (= M154), Q188 (≠ E175), H221 (= H208)
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
35% identity, 78% coverage: 19:232/274 of query aligns to 5:216/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F26), S38 (= S55), C40 (= C57), G41 (= G58), K42 (= K59), S43 (= S60), T44 (= T61), Q82 (= Q96), R129 (≠ K145), Q133 (= Q149), S135 (= S151), G136 (= G152), G137 (= G153), Q159 (≠ E175), H192 (= H208)
- binding magnesium ion: S43 (= S60), Q82 (= Q96)
8hprC Lpqy-sugabc in state 4 (see paper)
35% identity, 78% coverage: 19:232/274 of query aligns to 5:216/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F26), S38 (= S55), G39 (= G56), G41 (= G58), K42 (= K59), S43 (= S60), Q82 (= Q96), Q133 (= Q149), G136 (= G152), G137 (= G153), Q138 (≠ M154), H192 (= H208)
- binding magnesium ion: S43 (= S60), Q82 (= Q96)
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
35% identity, 74% coverage: 31:232/274 of query aligns to 17:225/375 of 2d62A
1g291 Malk (see paper)
34% identity, 77% coverage: 31:242/274 of query aligns to 14:231/372 of 1g291
- binding magnesium ion: D69 (≠ E86), E71 (≠ G88), K72 (≠ P89), K79 (vs. gap), D80 (vs. gap)
- binding pyrophosphate 2-: S38 (= S55), G39 (= G56), C40 (= C57), G41 (= G58), K42 (= K59), T43 (≠ S60), T44 (= T61)
Sites not aligning to the query:
8hplC Lpqy-sugabc in state 1 (see paper)
35% identity, 78% coverage: 19:232/274 of query aligns to 5:214/384 of 8hplC
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
37% identity, 77% coverage: 16:226/274 of query aligns to 1:221/232 of 1f3oA
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
36% identity, 77% coverage: 16:226/274 of query aligns to 1:221/230 of 1l2tA
- binding adenosine-5'-triphosphate: Y11 (≠ F26), S40 (= S55), G41 (= G56), S42 (≠ C57), G43 (= G58), K44 (= K59), S45 (= S60), T46 (= T61), F138 (vs. gap), Q145 (= Q149), S147 (= S151), G149 (= G153), Q150 (≠ M154), H204 (= H208)
2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
37% identity, 77% coverage: 31:241/274 of query aligns to 13:227/374 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)
37% identity, 77% coverage: 31:241/274 of query aligns to 14:228/371 of P68187
- A85 (≠ S99) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ H120) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V130) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ H133) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (= E135) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ T140) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G153) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D174) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
- R228 (= R241) 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.
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
37% identity, 77% coverage: 31:241/274 of query aligns to 13:227/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S55), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), Q81 (= Q96), R128 (≠ K145), A132 (≠ Q149), S134 (= S151), G136 (= G153), Q137 (≠ M154), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
Sites not aligning to the query:
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
37% identity, 77% coverage: 31:241/274 of query aligns to 13:227/371 of 3puxA
- binding adenosine-5'-diphosphate: G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (≠ K145), S134 (= S151), Q137 (≠ M154)
- binding beryllium trifluoride ion: S37 (= S55), G38 (= G56), K41 (= K59), Q81 (= Q96), S134 (= S151), G136 (= G153), H191 (= H208)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
Sites not aligning to the query:
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
37% identity, 77% coverage: 31:241/274 of query aligns to 13:227/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ A35), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (≠ K145), A132 (≠ Q149), S134 (= S151), Q137 (≠ M154)
- binding tetrafluoroaluminate ion: S37 (= S55), G38 (= G56), K41 (= K59), Q81 (= Q96), S134 (= S151), G135 (= G152), G136 (= G153), E158 (= E175), H191 (= H208)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
Sites not aligning to the query:
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
37% identity, 77% coverage: 31:241/274 of query aligns to 13:227/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ A35), G38 (= G56), C39 (= C57), G40 (= G58), K41 (= K59), S42 (= S60), T43 (= T61), R128 (≠ K145), A132 (≠ Q149), S134 (= S151), Q137 (≠ M154)
- binding magnesium ion: S42 (= S60), Q81 (= Q96)
Sites not aligning to the query:
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
37% identity, 77% coverage: 31:241/274 of query aligns to 11:225/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S55), G36 (= G56), C37 (= C57), G38 (= G58), K39 (= K59), S40 (= S60), T41 (= T61), R126 (≠ K145), A130 (≠ Q149), S132 (= S151), G134 (= G153), Q135 (≠ M154)
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)
37% identity, 77% coverage: 31:241/274 of query aligns to 14:228/369 of P19566
- L86 (= L100) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- P160 (= P176) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
- D165 (= D181) 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.
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
38% identity, 70% coverage: 36:226/274 of query aligns to 23:218/226 of 5xu1B
Query Sequence
>Synpcc7942_1236 FitnessBrowser__SynE:Synpcc7942_1236
MTAILPSTAATVNTGFLHFDCVGKTFPTPRGPYVAIEDVNLSVQQGEFICVIGHSGCGKS
TLLNLVSGFSQPTSGGVYLDGQPIQEPGPDRMVVFQNYSLLPWKSARDNIALAVKAARPH
LSTSEQRQVVDHHLELVGLTEAQHKRPDQLSGGMKQRVAIARALSIRPEVLILDEPFGAL
DAITKEELQEELLNIWEEARPTVLMITHDIDEALFLADRVVMMTNGPAATIGEVLEIPFD
RPREREAVVEDPRYAQLRTEALDFLYRRFAHDDD
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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