SitesBLAST
Comparing Synpcc7942_1490 FitnessBrowser__SynE:Synpcc7942_1490 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)
2i4bA Crystal structure of bicarbonate transport protein cmpa from synechocystis sp. Pcc 6803 in complex with bicarbonate and calcium (see paper)
30% identity, 56% coverage: 277:645/663 of query aligns to 6:400/401 of 2i4bA
P73452 Nitrate/nitrite binding protein NrtA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
29% identity, 55% coverage: 277:643/663 of query aligns to 60:441/446 of P73452
- W102 (= W319) binding
- Q155 (≠ N367) binding
- H196 (= H409) binding
- G240 (= G453) binding
- K269 (= K482) binding
2g29A Crystal structure of the periplasmic nitrate-binding protein nrta from synechocystis pcc 6803 (see paper)
29% identity, 55% coverage: 277:643/663 of query aligns to 4:385/385 of 2g29A
8hprD Lpqy-sugabc in state 4 (see paper)
40% identity, 33% coverage: 5:221/663 of query aligns to 3:216/362 of 8hprD
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q85), R129 (≠ K134), Q133 (= Q138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
8hprC Lpqy-sugabc in state 4 (see paper)
40% identity, 33% coverage: 5:221/663 of query aligns to 3:216/363 of 8hprC
- binding adenosine-5'-triphosphate: Y12 (≠ F14), S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q85), Q133 (= Q138), G136 (= G141), G137 (= G142), Q138 (≠ M143), H192 (= H197)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
8hplC Lpqy-sugabc in state 1 (see paper)
40% identity, 33% coverage: 5:221/663 of query aligns to 3:214/384 of 8hplC
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
41% identity, 30% coverage: 24:221/663 of query aligns to 21:225/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
43% identity, 32% coverage: 1:215/663 of query aligns to 14:224/378 of P69874
- C26 (≠ S13) mutation to A: Lower ATPase activity and transport efficiency.
- F27 (= F14) mutation to L: Lower ATPase activity and transport efficiency.
- F45 (= F37) mutation to L: Lower ATPase activity and transport efficiency.
- C54 (= C46) mutation to T: Loss of ATPase activity and transport.
- L60 (= L52) mutation to F: Lower ATPase activity and transport efficiency.
- L76 (= L68) mutation to P: Lower ATPase activity and transport efficiency.
- V135 (= V126) mutation to M: Loss of ATPase activity and transport.
- D172 (= D163) mutation to N: Loss of ATPase activity and transport.
Sites not aligning to the query:
- 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.
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)
38% identity, 33% coverage: 5:221/663 of query aligns to 4:217/393 of P9WQI3
- H193 (= H197) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.
1g291 Malk (see paper)
39% identity, 31% coverage: 20:226/663 of query aligns to 14:227/372 of 1g291
- binding magnesium ion: D69 (vs. gap), E71 (vs. gap), K72 (vs. gap), K79 (≠ P78), D80 (= D79)
- binding pyrophosphate 2-: S38 (= S44), G39 (= G45), C40 (= C46), G41 (= G47), K42 (= K48), T43 (≠ S49), T44 (= T50)
Sites not aligning to the query:
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
38% identity, 29% coverage: 29:221/663 of query aligns to 46:245/382 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)
38% identity, 29% coverage: 29:221/663 of query aligns to 46:245/382 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
1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
40% identity, 33% coverage: 5:226/663 of query aligns to 7:216/353 of 1vciA
7ahdC Opua (e190q) occluded (see paper)
37% identity, 29% coverage: 29:221/663 of query aligns to 46:245/260 of 7ahdC
- binding adenosine-5'-triphosphate: S61 (= S44), G62 (= G45), G64 (= G47), K65 (= K48), S66 (= S49), T67 (= T50), Q111 (= Q85), K161 (≠ A137), Q162 (= Q138), S164 (= S140), G166 (= G142), M167 (= M143), Q188 (≠ E164), H221 (= H197)
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, 33% coverage: 5:226/663 of query aligns to 3:220/374 of 2awnB
P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 33% coverage: 5:226/663 of query aligns to 4:221/371 of P68187
- A85 (≠ S88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ P111) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (= V119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ H122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ Q124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ G129) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- G137 (= G142) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
- D158 (= D163) 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)
39% identity, 33% coverage: 5:226/663 of query aligns to 3:220/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: W12 (≠ F14), S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q85), R128 (≠ K134), A132 (≠ Q138), S134 (= S140), G136 (= G142), Q137 (≠ M143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
39% identity, 33% coverage: 5:226/663 of query aligns to 3:220/371 of 3puxA
- binding adenosine-5'-diphosphate: W12 (≠ F14), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K134), S134 (= S140), Q137 (≠ M143)
- binding beryllium trifluoride ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S140), G136 (= G142), H191 (= H197)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
39% identity, 33% coverage: 5:226/663 of query aligns to 3:220/371 of 3puwA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K134), A132 (≠ Q138), S134 (= S140), Q137 (≠ M143)
- binding tetrafluoroaluminate ion: S37 (= S44), G38 (= G45), K41 (= K48), Q81 (= Q85), S134 (= S140), G135 (= G141), G136 (= G142), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
39% identity, 33% coverage: 5:226/663 of query aligns to 3:220/371 of 3puvA
- binding adenosine-5'-diphosphate: W12 (≠ F14), V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K134), A132 (≠ Q138), S134 (= S140), Q137 (≠ M143)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
Query Sequence
>Synpcc7942_1490 FitnessBrowser__SynE:Synpcc7942_1490
MSLFVAVENIEKSFPLSGGNEYLALKGIDLEIKQGEFISLIGHSGCGKSTLLNLIAGLEL
PTDGAVSLEGQQITAPGPDRMVVFQNYSLFPWLTVRENIALAVDEVLRDLPKEERQAIVE
EHIQLVGLGHAADKPPAQLSGGMKQRVAIARGLATRPKLLLLDEPFGALDALTRGNLQEK
LMQICEENHVTAVMVTHDVDEAVLLSDRIVMLTNGPGSKIGGILEVDIPRPRKRMDVVHH
PSYYSLRSEIIYFLNQQKRVKKLNARKVTTVARHGLEKVNLEIGYVPLMACAPLVVAQEK
AFFAKHGLDEVSLVRETSWRGIVDGLTENYLDAAQMPAGMPVWMSVGGQGGSPLPIVSSL
TMSRNGNGITLSKALYDEGIQTVDDFRNLLRSTADKQHIMGIVHPASMHNLLLRYWLAAN
QIDPDRDVQLRTIPPAQMVADLKDGTIDGYCIGEPWNAWAAQKEIGFTIASDLEIWNGHP
GKVLGVREDWANRYPNSHVALVKALLEACQYCEDPANWDELRELLSDRRYLSCPKEYIQF
SQSTADDLAVPHHRFAGAGVNRPSRTEHLWMMTQLARWGDVPFPRNWVEILERVCRVGVF
STAARELGLSEVVNYQRSTPVELFDGVPFNAEDPIAYLNSLPIHRDFSVAEIALDQPRPI
AAA
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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