SitesBLAST
Comparing Synpcc7942_1237 FitnessBrowser__SynE:Synpcc7942_1237 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)
P73452 Nitrate/nitrite binding protein NrtA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
29% identity, 56% coverage: 275:646/659 of query aligns to 58:443/446 of P73452
- W102 (= W318) binding
- Q155 (≠ G366) binding
- H196 (≠ P407) binding
- G240 (= G451) binding
- K269 (= K480) binding
2g29A Crystal structure of the periplasmic nitrate-binding protein nrta from synechocystis pcc 6803 (see paper)
29% identity, 56% coverage: 275:644/659 of query aligns to 2:385/385 of 2g29A
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, 34% coverage: 5:231/659 of query aligns to 4:226/393 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.
2i4bA Crystal structure of bicarbonate transport protein cmpa from synechocystis sp. Pcc 6803 in complex with bicarbonate and calcium (see paper)
27% identity, 56% coverage: 277:645/659 of query aligns to 6:399/401 of 2i4bA
8hplC Lpqy-sugabc in state 1 (see paper)
43% identity, 30% coverage: 24:221/659 of query aligns to 16:214/384 of 8hplC
Sites not aligning to the query:
8hprD Lpqy-sugabc in state 4 (see paper)
43% identity, 30% coverage: 24:221/659 of query aligns to 18:216/362 of 8hprD
- binding adenosine-5'-triphosphate: S38 (= S44), C40 (= C46), G41 (= G47), K42 (= K48), S43 (= S49), T44 (= T50), Q82 (= Q85), R129 (≠ K134), Q133 (≠ E138), S135 (= S140), G136 (= G141), G137 (= G142), Q159 (≠ E164), H192 (= H197)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
Sites not aligning to the query:
8hprC Lpqy-sugabc in state 4 (see paper)
43% identity, 30% coverage: 24:221/659 of query aligns to 18:216/363 of 8hprC
- binding adenosine-5'-triphosphate: S38 (= S44), G39 (= G45), G41 (= G47), K42 (= K48), S43 (= S49), Q82 (= Q85), Q133 (≠ E138), G136 (= G141), G137 (= G142), Q138 (≠ M143), H192 (= H197)
- binding magnesium ion: S43 (= S49), Q82 (= Q85)
Sites not aligning to the query:
2d62A Crystal structure of multiple sugar binding transport atp- binding protein
38% identity, 31% coverage: 20:226/659 of query aligns to 17:230/375 of 2d62A
P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
40% identity, 34% coverage: 10:233/659 of query aligns to 23:241/378 of P69874
- C26 (≠ V13) 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.
1g291 Malk (see paper)
37% identity, 31% coverage: 20:226/659 of query aligns to 14:227/372 of 1g291
- binding magnesium ion: D69 (≠ E75), E71 (≠ G77), K72 (≠ P78), K79 (vs. gap), D80 (vs. gap)
- 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)
36% identity, 31% coverage: 16:221/659 of query aligns to 33:245/382 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
7aheC Opua inhibited inward facing (see paper)
36% identity, 31% coverage: 16:221/659 of query aligns to 33:245/382 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
7ahdC Opua (e190q) occluded (see paper)
35% identity, 31% coverage: 16:221/659 of query aligns to 33:245/260 of 7ahdC
- binding adenosine-5'-triphosphate: T39 (≠ Y22), S61 (= S44), G62 (= G45), G64 (= G47), K65 (= K48), S66 (= S49), T67 (= T50), Q111 (= Q85), K161 (≠ H137), Q162 (≠ E138), 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)
38% identity, 32% coverage: 20:232/659 of query aligns to 13:227/374 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)
38% identity, 32% coverage: 20:232/659 of query aligns to 13:227/371 of 3puyA
- binding phosphoaminophosphonic acid-adenylate ester: S37 (= S44), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), Q81 (= Q85), R128 (≠ K134), A132 (≠ E138), S134 (= S140), G136 (= G142), Q137 (≠ M143), E158 (= E164), H191 (= H197)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
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, 32% coverage: 20:232/659 of query aligns to 13:227/371 of 3puxA
- binding adenosine-5'-diphosphate: 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)
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, 32% coverage: 20:232/659 of query aligns to 13:227/371 of 3puwA
- binding adenosine-5'-diphosphate: V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K134), A132 (≠ E138), 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)
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, 32% coverage: 20:232/659 of query aligns to 13:227/371 of 3puvA
- binding adenosine-5'-diphosphate: V17 (≠ A24), G38 (= G45), C39 (= C46), G40 (= G47), K41 (= K48), S42 (= S49), T43 (= T50), R128 (≠ K134), A132 (≠ E138), S134 (= S140), Q137 (≠ M143)
- binding magnesium ion: S42 (= S49), Q81 (= Q85)
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, 32% coverage: 20:232/659 of query aligns to 14:228/371 of P68187
- A85 (≠ S88) mutation to M: Suppressor of EAA loop mutations in MalFG.
- K106 (≠ D109) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V114 (≠ I119) mutation to C: Suppressor of EAA loop mutations in MalFG.
- V117 (≠ T122) mutation to M: Suppressor of EAA loop mutations in MalFG.
- E119 (≠ D124) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
- A124 (≠ R129) 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.
- R228 (= R232) 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.
1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
38% identity, 32% coverage: 20:232/659 of query aligns to 11:225/367 of 1q12A
- binding adenosine-5'-triphosphate: S35 (= S44), G36 (= G45), C37 (= C46), G38 (= G47), K39 (= K48), S40 (= S49), T41 (= T50), R126 (≠ K134), A130 (≠ E138), S132 (= S140), G134 (= G142), Q135 (≠ M143)
Sites not aligning to the query:
Query Sequence
>Synpcc7942_1237 FitnessBrowser__SynE:Synpcc7942_1237
MSVFLAVDHVHQVFDLPGGGQYIALKDVSLNIRPGEFISLIGHSGCGKSTLLNLIAGLAQ
PSSGGIILEGRQVTEPGPDRMVVFQNYSLLPWRTVRQNIALAVDSVLHDRNRTERRTIIE
ETIDLVGLRAAADKYPHEISGGMKQRVAIARGLAIRPKLLLLDEPFGALDALTRGNLQEQ
LMRICQEAGVTAVMVTHDVDEALLLSDRVVMLTNGPAAQIGQILEVDFPRPRQRLEMMET
PHYYDLRNELINFLQQQRRAKRRAKAAAPAPAVAASQQKTVRLGFLPGNDCAPLAIAQEL
GLFQDLGLSVELQSFLTWEALEDSIRLGQLEGALMMAAQPLAMTMGLGGHRPFAIATPLT
VSRNGGAIALSRRYLNAGVRSLEDLCQFLAATPQRLRLAIPDPIAMPALLLRYWLASAGL
NPEQDVELVGMSPYEMVEALKAGDIDGFAAGEMRIALAVQAGAAYVLATDLDIWAGHPEK
VLGLPEAWLQVNPETAIALCSALLKAGELCDDPRQRDRIVEVLQQPQYLGSAAGTVLQRY
FDFGLGDEPTQILRFNQFHVDQANYPNPLEGTWLLTQLCRWGLTPLPKNRQELLDRVYRR
DIYEAAIAAVGFPLITPSQRGFELFDAVPFDPDSPLRYLEQFEIKAPIQVAPIPLATSA
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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