SitesBLAST
Comparing 8499436 DvMF_0208 EAL domain protein (RefSeq) 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)
Q55434 Phytochrome-like protein cph2; Bacteriophytochrome cph2 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
41% identity, 32% coverage: 494:734/762 of query aligns to 609:850/1276 of Q55434
Sites not aligning to the query:
- 129 C→S: Holoprotein exhibits no photochromic activity.
- 130 H→F: Chromophore ligating activity (in vitro) is 30-40% lower than wild-type.; H→Q: Chromophore ligating activity (in vitro) is about 10% more efficient than wild-type.
4rnhA Pamora tandem diguanylate cyclase - phosphodiesterase, c-di-gmp complex (see paper)
40% identity, 32% coverage: 494:736/762 of query aligns to 174:417/423 of 4rnhA
- binding 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one): Q193 (= Q514), L209 (= L529), L210 (= L530), R211 (= R531), P222 (= P542), N266 (= N586), D328 (= D648), R352 (= R672), G386 (= G705), E388 (= E707), G406 (= G725), Y407 (= Y726)
- binding magnesium ion: E207 (= E527), N266 (= N586), E298 (= E618), D328 (= D648)
8arvA Structure of the eal domain of bifa from pseudomonas aeruginosa (see paper)
42% identity, 32% coverage: 494:734/762 of query aligns to 1:242/255 of 8arvA
5m3cB Structure of the hybrid domain (ggdef-eal) of pa0575 from pseudomonas aeruginosa pao1 at 2.8 ang. With gtp and ca2+ bound to the active site of the ggdef domain (see paper)
40% identity, 32% coverage: 494:734/762 of query aligns to 174:415/426 of 5m3cB
Sites not aligning to the query:
- binding calcium ion: 38, 39, 81
- binding guanosine-5'-triphosphate: 41, 42, 43, 46, 51, 55, 58, 80, 81, 151, 155
3n3tB Crystal structure of putative diguanylate cyclase/phosphodiesterase complex with cyclic di-gmp (see paper)
40% identity, 31% coverage: 494:731/762 of query aligns to 5:245/261 of 3n3tB
- binding 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one): Q24 (= Q514), L40 (= L529), V41 (≠ L530), R42 (= R531), P53 (= P542), N99 (= N586), D161 (= D648), Q185 (≠ R672), E218 (= E704), G219 (= G705), E221 (= E707), G239 (= G725), N240 (≠ Y726)
- binding magnesium ion: E38 (= E527), N99 (= N586), E131 (= E618), D161 (= D648), D161 (= D648), D162 (= D649), E218 (= E704)
5m1tA Pamucr phosphodiesterase, c-di-gmp complex (see paper)
39% identity, 32% coverage: 494:738/762 of query aligns to 2:247/247 of 5m1tA
- binding 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one): Q21 (= Q514), E35 (= E527), L37 (= L529), R39 (= R531), P50 (= P542), L54 (≠ V546), V70 (= V562), N94 (= N586), R180 (= R672), G214 (= G705), E216 (= E707), G234 (= G725), F235 (≠ Y726)
- binding magnesium ion: E35 (= E527), N94 (= N586), E126 (= E618), D156 (= D648), D156 (= D648), D157 (= D649), E213 (= E704)
3qnqD Crystal structure of the transporter chbc, the iic component from the n,n'-diacetylchitobiose-specific phosphotransferase system (see paper)
27% identity, 54% coverage: 46:454/762 of query aligns to 10:424/436 of 3qnqD
P76129 Oxygen sensor protein DosP; Direct oxygen-sensing phosphodiesterase; Direct oxygen sensor protein; Ec DOS; Heme-regulated cyclic di-GMP phosphodiesterase; EC 3.1.4.52 from Escherichia coli (strain K12) (see 6 papers)
34% identity, 32% coverage: 499:744/762 of query aligns to 544:790/799 of P76129
- H582 (= H533) mutation to A: Loss of cAMP PDE activity.
- H586 (≠ Y537) mutation to A: Loss of cAMP PDE activity.
Sites not aligning to the query:
- 69 mutation H->A,G: Loss of heme binding.
- 75 mutation H->A,G: No loss of heme binding.
- 87 mutation M->A,I: Ferrous heme iron changes from an exclusively hexacoordinate low-spin form to an exclusively pentacoordinate high-spin form. Ferric heme iron remains hexacoordinate but becomes a mixture of high and low spin. Increases c-di-GMP PDE activity 7-fold in absence of O(2), CO or NO, no additional increase upon addition of gases (M-A only).; M→H: No change in heme coordination; increases c-di-GMP PDE activity 2-fold in absence of O(2), CO or NO, and 2-fold more upon addition of gases.
- 89 mutation R->A,E,I: The Fe(2+)-O(2) form loses c-di-GMP PDE activity, due to reduced O(2) affinity and/or increased auto-oxidation. NO and CO forms are less affected.
- 91 L→F: Alters O(2) binding, increases auto-oxidation.; L→T: Increases auto-oxidation.
- 107 L→F: Significantly reduces heme-binding affinity; increases auto-oxidation.; L→T: Increases auto-oxidation.
Q9HX69 Cyclic di-GMP phosphodiesterase RocR; c-di-GMP PDE; Response regulator RocR; EC 3.1.4.52 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 3 papers)
36% identity, 31% coverage: 506:743/762 of query aligns to 153:391/392 of Q9HX69
- Q161 (= Q514) mutation to A: 5.1-fold decrease in kcat.
- E175 (= E527) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- R179 (= R531) mutation to A: 29.1-fold decrease in kcat.
- N233 (= N586) binding ; mutation to A: Loss of activity. Activity can be fully restored at elevated Mg(2+) concentrations (up to 500 mM).
- E265 (= E618) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- T267 (= T620) mutation to A: 13.4-fold decrease in kcat.
- E268 (= E621) mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).; mutation to Q: 446-fold decrease in kcat.
- R286 (= R639) mutation to W: Thermostable. Shows lower enzymatic activity.
- D295 (= D648) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- D296 (= D649) mutation to A: 33.5-fold decrease in kcat.
- F297 (= F650) mutation to A: 33.5-fold decrease in kcat.
- S302 (≠ A655) mutation to A: 4.8-fold decrease in kcat.
- K316 (= K669) mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- D318 (= D671) mutation to A: 8.4-fold decrease in kcat.
- E352 (= E704) mutation E->A,C: Loss of activity.; mutation to D: 30000-fold decrease in kcat.; mutation to Q: 61000-fold decrease in kcat.
- E355 (= E707) mutation to A: 1.3-fold decrease in kcat.
- Q372 (= Q724) mutation to A: 8.4-fold decrease in kcat.
Sites not aligning to the query:
- 56 D→N: 5.2-fold decrease in kcat.
3sy8B Crystal structure of the response regulator rocr (see paper)
35% identity, 31% coverage: 506:743/762 of query aligns to 153:391/392 of 3sy8B
3sy8D Crystal structure of the response regulator rocr (see paper)
35% identity, 32% coverage: 506:747/762 of query aligns to 126:368/371 of 3sy8D
6hq7A Structure of eal enzyme bd1971 - cgmp bound form (see paper)
32% identity, 33% coverage: 480:732/762 of query aligns to 102:366/377 of 6hq7A
Sites not aligning to the query:
- binding cyclic guanosine monophosphate: 12, 31, 42, 51, 52, 53, 54, 55, 62, 63, 64
4hjfA Eal domain of phosphodiesterase pdea in complex with c-di-gmp and ca++
35% identity, 32% coverage: 494:740/762 of query aligns to 6:254/263 of 4hjfA
- binding 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one): Q25 (= Q514), L41 (= L529), A42 (≠ L530), R43 (= R531), P54 (= P542), L58 (≠ V546), M74 (≠ V562), N100 (= N586), S102 (≠ A588), R186 (= R672), G220 (= G705), E222 (= E707), G240 (= G725), F241 (≠ Y726)
- binding calcium ion: E39 (= E527), N100 (= N586), E132 (= E618), D162 (= D648), D162 (= D648), E219 (= E704)
3u2eA Eal domain of phosphodiesterase pdea in complex with 5'-pgpg and mg++
35% identity, 32% coverage: 494:740/762 of query aligns to 4:252/260 of 3u2eA
- binding magnesium ion: E37 (= E527), N98 (= N586), E130 (= E618), D160 (= D648), D160 (= D648), D161 (= D649), E217 (= E704)
- binding : Q23 (= Q514), L39 (= L529), A40 (≠ L530), R41 (= R531), P52 (= P542), L56 (≠ V546), M72 (≠ V562), N98 (= N586), S100 (≠ A588), D160 (= D648), D161 (= D649), R184 (= R672), E217 (= E704), E220 (= E707), G238 (= G725), F239 (≠ Y726)
6hq5A Structure of eal enzyme bd1971 - camp and cyclic-di-gmp bound form (see paper)
31% identity, 31% coverage: 494:732/762 of query aligns to 119:365/376 of 6hq5A
- binding 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one): Q138 (= Q514), L154 (= L529), R156 (= R531), N219 (= N586), D280 (= D648), R304 (= R672), G338 (= G705), E340 (= E707), G358 (= G725), Y359 (= Y726)
- binding calcium ion: E152 (= E527), N219 (= N586), E251 (= E618), D280 (= D648), D280 (= D648), D281 (= D649), D303 (= D671), E337 (= E704)
Sites not aligning to the query:
- binding adenosine-3',5'-cyclic-monophosphate: 13, 32, 52, 53, 54, 55, 56, 63, 64, 65
4lj3A Crystal structure of the eal domain of c-di-gmp specific phosphodiesterase yaha in complex with substratE C-di-gmp and ca++ (see paper)
35% identity, 29% coverage: 512:732/762 of query aligns to 18:244/256 of 4lj3A
- binding 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one): Q24 (≠ R518), L40 (= L529), V41 (≠ L530), R42 (= R531), P53 (= P542), N97 (= N586), D159 (= D648), K183 (≠ R672), G217 (= G705), E219 (= E707), G237 (= G725), Y238 (= Y726), P243 (= P731)
- binding calcium ion: E38 (= E527), N97 (= N586), E129 (= E618), D159 (= D648), D160 (= D649), E216 (= E704)
- binding trans-4-(hydroxymethyl)cyclohexanol: V26 (vs. gap), T35 (≠ H524), G36 (= G525), H93 (≠ V582), E129 (= E618), F178 (≠ T667), F234 (≠ V722)
Q9I0R8 Cyclic di-GMP phosphodiesterase PA2567; c-di-GMP PDE; EC 3.1.4.52 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
34% identity, 32% coverage: 492:732/762 of query aligns to 335:576/587 of Q9I0R8
- E464 (= E621) mutation to A: Does not perturb the oligomeric state and does not affect kcat.
P21514 Cyclic di-GMP phosphodiesterase PdeL; EC 3.1.4.52 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 29% coverage: 512:732/762 of query aligns to 121:347/362 of P21514
- Q127 (≠ R518) binding
- E141 (= E527) binding
- VR 144:145 (≠ LR 530:531) binding
- N200 (= N586) binding ; binding
- F206 (≠ L592) mutation to S: Increases catalytic activity.
- E232 (= E618) binding
- F249 (≠ L635) mutation to L: Increases catalytic activity.
- D262 (= D648) binding ; binding
- D263 (= D649) mutation to N: Loss of activity.
- K286 (≠ R672) binding
- S298 (≠ N683) mutation to W: Slow monomer-dimer exchange. Equilibrium largely on the monomeric side, in particular in the presence of substrate. Strong decrease in activity.
- G299 (≠ E684) mutation to S: Increases catalytic activity.
- EGVE 319:322 (= EGVE 704:707) binding
- Y341 (= Y726) binding
Sites not aligning to the query:
- 60 K→A: Does not bind to the PdeL box.
4lykA Crystal structure of the eal domain of c-di-gmp specific phosphodiesterase yaha in complex with activating cofactor mg++ (see paper)
35% identity, 29% coverage: 512:732/762 of query aligns to 15:241/253 of 4lykA
- binding trans-4-(hydroxymethyl)cyclohexanol: V23 (vs. gap), T32 (≠ H524), G33 (= G525), H90 (≠ V582), V124 (≠ E616), E126 (= E618), F175 (≠ T667), F231 (≠ V722)
- binding magnesium ion: E35 (= E527), N94 (= N586), E126 (= E618), D156 (= D648)
5mfuA Pa3825-eal mn-pgpg structure (see paper)
37% identity, 31% coverage: 493:732/762 of query aligns to 1:241/254 of 5mfuA
- binding guanosine-5'-monophosphate: Q21 (= Q514), L37 (= L529), M38 (≠ L530), R39 (= R531), R49 (≠ A541), P50 (= P542), D51 (≠ P543), N94 (= N586), D156 (= D648), D157 (= D649), Q180 (≠ R672), E213 (= E704), G214 (= G705), E216 (= E707), G234 (= G725), Y235 (= Y726)
- binding manganese (ii) ion: E35 (= E527), N94 (= N586), E126 (= E618), D156 (= D648)
Query Sequence
>8499436 DvMF_0208 EAL domain protein (RefSeq)
MKAGSAEETVAPSTGGERIMGDAVADNAANRAAPWWRPLAAVFADVTERVADQPVVIAVQ
RALALVLPLVTVGAFALMVRHTPFPLLRAALDALFGPAWITMGDALVSGTFGIASLAVLC
AFSGTMAMVYNQRRGGQFVSPVMSAIVVLACFFVVTNPASDMPWRDMFSMDRGLLLAFMV
SVGGAWLFLRLSDVKRLQLPLEAVGHDPVVRDILTVMPAGMLTIVAFGLLRVGLVDSGIP
DLHGALRSGMTRPFIEGGNTLGLGLLYTGLSQVLWFFGAHGPNLLFPIEDAIFAPAGAAN
AAALATGQVPPFVLTKTFFDVFTRMGGSGSTLCLIAAILYASRDSGTRRLALVALLPALC
NVNEPLLFGLPLVMNPVYLIPFLLVPLAQTAAAHAATLLHLVPYTLPDVVWTTPPLLNGY
AATGSVAGSLMQALNLGLGVALYLPFVRASDALRERHGRHILAELLRTASGSEVGPAGRK
CIDRPGEQGRIASSLANDLAAALARNGEVFLEYQPQIRMDGRAHGAEALLRWHHPAYGRI
APPITVALAEDTGIIDRLGMFVLHRACARRVAWTGEVPDGFVMSVNVAPRQLQNPRFDRD
VLAVLARTGLAPHLLELELTESTVLLPDARTVAALRRLRAAGVRVAIDDFGMGHASLRYL
RDFPVDTVKIDRSLTEASHGDVNEHIVRSIVELARSLDITTLVEGVERREQFERFVELGC
LVFQGYLFSRPVRAVQCLEVVSGWGGHAAAPEQAVPDIPKGA
Or try a new SitesBLAST search
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