SitesBLAST
Comparing 7026215 FitnessBrowser__ANA3:7026215 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)
8arvA Structure of the eal domain of bifa from pseudomonas aeruginosa (see paper)
31% identity, 40% coverage: 363:603/610 of query aligns to 1:248/255 of 8arvA
3qnqD Crystal structure of the transporter chbc, the iic component from the n,n'-diacetylchitobiose-specific phosphotransferase system (see paper)
35% identity, 28% coverage: 148:317/610 of query aligns to 236:418/436 of 3qnqD
Sites not aligning to the query:
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)
31% identity, 41% coverage: 348:599/610 of query aligns to 528:786/799 of P76129
- H582 (≠ K401) mutation to A: Loss of cAMP PDE activity.
- H586 (= H404) 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.
3u2eA Eal domain of phosphodiesterase pdea in complex with 5'-pgpg and mg++
32% identity, 40% coverage: 360:606/610 of query aligns to 1:256/260 of 3u2eA
- binding magnesium ion: E37 (= E395), N98 (= N452), E130 (= E481), D160 (= D511), D160 (= D511), D161 (= D512), E217 (= E567)
- binding : Q23 (= Q381), L39 (= L397), A40 (≠ I398), R41 (= R399), P52 (≠ G409), L56 (≠ I413), M72 (≠ V429), N98 (= N452), S100 (≠ D454), D160 (= D511), D161 (= D512), R184 (= R535), E217 (= E567), E220 (= E570), G238 (= G588), F239 (≠ W589)
4hjfA Eal domain of phosphodiesterase pdea in complex with c-di-gmp and ca++
32% identity, 40% coverage: 360:606/610 of query aligns to 3:258/263 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 (= Q381), L41 (= L397), A42 (≠ I398), R43 (= R399), P54 (≠ G409), L58 (≠ I413), M74 (≠ V429), N100 (= N452), S102 (≠ D454), R186 (= R535), G220 (= G568), E222 (= E570), G240 (= G588), F241 (≠ W589)
- binding calcium ion: E39 (= E395), N100 (= N452), E132 (= E481), D162 (= D511), D162 (= D511), E219 (= E567)
4rnhA Pamora tandem diguanylate cyclase - phosphodiesterase, c-di-gmp complex (see paper)
30% identity, 41% coverage: 348:599/610 of query aligns to 159:417/423 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 (= Q381), L209 (= L397), L210 (≠ I398), R211 (= R399), P222 (= P410), N266 (= N452), D328 (= D511), R352 (= R535), G386 (= G568), E388 (= E570), G406 (= G588), Y407 (≠ W589)
- binding magnesium ion: E207 (= E395), N266 (= N452), E298 (= E481), D328 (= D511)
3n3tB Crystal structure of putative diguanylate cyclase/phosphodiesterase complex with cyclic di-gmp (see paper)
30% identity, 39% coverage: 362:600/610 of query aligns to 4:247/261 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 (= Q381), L40 (= L397), V41 (≠ I398), R42 (= R399), P53 (≠ G409), N99 (= N452), D161 (= D511), Q185 (≠ R535), E218 (= E567), G219 (= G568), E221 (= E570), G239 (= G588), N240 (≠ W589)
- binding magnesium ion: E38 (= E395), N99 (= N452), E131 (= E481), D161 (= D511), D161 (= D511), D162 (= D512), E218 (= E567)
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)
29% identity, 41% coverage: 348:596/610 of query aligns to 159:414/426 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
Q55434 Phytochrome-like protein cph2; Bacteriophytochrome cph2 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
27% identity, 42% coverage: 344:597/610 of query aligns to 590:850/1276 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.
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)
25% identity, 50% coverage: 305:607/610 of query aligns to 285:587/587 of Q9I0R8
- E464 (= E484) mutation to A: Does not perturb the oligomeric state and does not affect kcat.
5yrpA Crystal structure of the eal domain of mycobacterium smegmatis dcpa (see paper)
30% identity, 37% coverage: 376:603/610 of query aligns to 2:217/224 of 5yrpA
6hq7A Structure of eal enzyme bd1971 - cgmp bound form (see paper)
29% identity, 36% coverage: 375:593/610 of query aligns to 133:364/377 of 6hq7A
Sites not aligning to the query:
- binding cyclic guanosine monophosphate: 12, 31, 42, 51, 52, 53, 54, 55, 62, 63, 64, 103, 104, 106
6hq5A Structure of eal enzyme bd1971 - camp and cyclic-di-gmp bound form (see paper)
29% identity, 36% coverage: 375:593/610 of query aligns to 132:363/376 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 (= Q381), L154 (= L397), R156 (= R399), N219 (= N452), D280 (= D511), R304 (= R535), G338 (= G568), E340 (= E570), G358 (= G588), Y359 (≠ W589)
- binding calcium ion: E152 (= E395), N219 (= N452), E251 (= E481), D280 (= D511), D280 (= D511), D281 (= D512), D303 (= D534), E337 (= E567)
Sites not aligning to the query:
- binding adenosine-3',5'-cyclic-monophosphate: 13, 32, 52, 53, 54, 55, 56, 63, 64, 65
5mf5A Pa3825-eal mg-cdg structure (see paper)
31% identity, 37% coverage: 373:596/610 of query aligns to 13:242/256 of 5mf5A
- 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 (= Q381), L37 (= L397), M38 (≠ I398), R39 (= R399), R49 (≠ K408), P50 (≠ G409), D51 (≠ P410), N94 (= N452), Q180 (≠ R535), G214 (= G568), E216 (= E570), G234 (= G588), Y235 (≠ W589), P240 (≠ A594)
- binding magnesium ion: E35 (= E395), V36 (≠ A396), N94 (= N452), N94 (= N452), E126 (≠ N476), D156 (= D511), D157 (= D512), D179 (= D534)
5mfuA Pa3825-eal mn-pgpg structure (see paper)
31% identity, 37% coverage: 373:596/610 of query aligns to 13:242/254 of 5mfuA
- binding guanosine-5'-monophosphate: Q21 (= Q381), L37 (= L397), M38 (≠ I398), R39 (= R399), R49 (≠ K408), P50 (≠ G409), D51 (≠ P410), N94 (= N452), D156 (= D511), D157 (= D512), Q180 (≠ R535), E213 (= E567), G214 (= G568), E216 (= E570), G234 (= G588), Y235 (≠ W589)
- binding manganese (ii) ion: E35 (= E395), N94 (= N452), E126 (≠ N476), D156 (= D511)
5m1tA Pamucr phosphodiesterase, c-di-gmp complex (see paper)
27% identity, 37% coverage: 375:599/610 of query aligns to 15:245/247 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 (= Q381), E35 (= E395), L37 (= L397), R39 (= R399), P50 (≠ G409), L54 (≠ I413), V70 (= V429), N94 (= N452), R180 (= R535), G214 (= G568), E216 (= E570), G234 (= G588), F235 (≠ W589)
- binding magnesium ion: E35 (= E395), N94 (= N452), E126 (= E481), D156 (= D511), D156 (= D511), D157 (= D512), E213 (= E567)
P24400 PTS system lactose-specific EIICB component; EIICB-Lac; EII-Lac; EC 2.7.1.207 from Lacticaseibacillus casei (Lactobacillus casei) (see paper)
32% identity, 24% coverage: 177:325/610 of query aligns to 266:417/577 of P24400
Sites not aligning to the query:
- 483 modified: Phosphocysteine; by EIIA; mutation C->H,S: Unable to be phosphorylated.
3pjuA Structure of pseudomonas fluorescence lapd eal domain complexed with c-di-gmp, p6522 (see paper)
28% identity, 36% coverage: 377:596/610 of query aligns to 28:247/249 of 3pjuA
- 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): Q32 (= Q381), K47 (≠ E395), L49 (= L397), S50 (≠ I398), R51 (= R399), A62 (≠ G409), G63 (≠ P410), L66 (≠ I413), M82 (≠ V429), N100 (= N452), Q161 (≠ D511), R162 (≠ D512), R219 (≠ G568), E221 (= E570), G239 (= G588), Q240 (≠ W589)
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)
27% identity, 37% coverage: 374:596/610 of query aligns to 154:381/392 of Q9HX69
- Q161 (= Q381) mutation to A: 5.1-fold decrease in kcat.
- E175 (= E395) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- R179 (= R399) mutation to A: 29.1-fold decrease in kcat.
- N233 (= N452) binding ; mutation to A: Loss of activity. Activity can be fully restored at elevated Mg(2+) concentrations (up to 500 mM).
- E265 (= E481) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- T267 (≠ L483) mutation to A: 13.4-fold decrease in kcat.
- E268 (= E484) 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 (≠ K502) mutation to W: Thermostable. Shows lower enzymatic activity.
- D295 (= D511) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- D296 (= D512) mutation to A: 33.5-fold decrease in kcat.
- F297 (= F513) mutation to A: 33.5-fold decrease in kcat.
- S302 (= S518) mutation to A: 4.8-fold decrease in kcat.
- K316 (= K532) mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- D318 (= D534) mutation to A: 8.4-fold decrease in kcat.
- E352 (= E567) mutation E->A,C: Loss of activity.; mutation to D: 30000-fold decrease in kcat.; mutation to Q: 61000-fold decrease in kcat.
- E355 (= E570) mutation to A: 1.3-fold decrease in kcat.
- Q372 (= Q587) mutation to A: 8.4-fold decrease in kcat.
Sites not aligning to the query:
- 56 D→N: 5.2-fold decrease in kcat.
6ij2A Crystal structure of a standalone versatile eal protein from vibrio cholerae o395 - 5'-pgpg bound form (see paper)
29% identity, 37% coverage: 375:600/610 of query aligns to 4:225/236 of 6ij2A
- binding calcium ion: E24 (= E395), N74 (= N452), E107 (= E481), T109 (≠ L483), D137 (= D511), D137 (= D511), D137 (= D511), D138 (= D512), D138 (= D512), D138 (= D512), S141 (≠ T515), Y143 (≠ F517), E194 (= E567)
- binding : Q10 (= Q381), L26 (= L397), V27 (≠ I398), R28 (= R399), I39 (≠ D414), N74 (= N452), L76 (≠ D454), D137 (= D511), M161 (≠ R535), G195 (= G568), E197 (= E570), G215 (= G588), Y216 (≠ W589)
Query Sequence
>7026215 FitnessBrowser__ANA3:7026215
MQLSKIFPLLALISLSFHFAKYLQLSAIVVCSLSLSILLAINAQDTGNVFNLDYVRAILA
DPRIAVLPIISAYLLRFLSAWKGLQLIKAKALSRYLKQHLNLFFPIVIGFIGLFAVVAEA
SIFLEWLFAPFIEGLQQASLGVQLFMRILLTHVLWCFGVHGDNAYLLLIGVDNGLMQLVP
HLTASQFMDLFILYGGSGATLSLIIAIFIGAKDSATRHIAKIATPFAIFNINEILIYGLP
IIFNPRLLVPFILSPLVNFILAYSAIHVGLLSFEGHSFPWITPPLLNAYIASGHMSAVFF
QVLLIGLGVLIYLPFVRRFSLMSEHYEFDSELIKRVQFQADIDRMTEQHYSQQQSESLKA
ELNLEKTIKEVLAGELQLHYQPKIALSTNHVVGYEALIRLKDEHGKLKGPYFIDAFQRAG
YSHIIDRFVINTVAEDLARWELEGFYPKVSINIDPNNITDPQLLATMNERLGSVANRVEI
EMLESAFMLDLNRIDNSMKQLKQHGFSFFLDDFGTGFSSLSLLSRINVDGIKLDRSILAN
TCEPKGRTLYLQICKLCNSLGFSLIAEGVETPEEAEFVNAAGVSYVQGWLYAKAMPGPEA
KAFWLERNSE
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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