SitesBLAST
Comparing 5208407 FitnessBrowser__PV4:5208407 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)
35% identity, 34% coverage: 422:662/707 of query aligns to 1:248/255 of 8arvA
4rnhA Pamora tandem diguanylate cyclase - phosphodiesterase, c-di-gmp complex (see paper)
31% identity, 34% coverage: 420:658/707 of query aligns to 172:417/423 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 (= Q440), L209 (= L456), L210 (= L457), R211 (= R458), P222 (≠ G468), N266 (= N511), D328 (= D570), R352 (= R594), G386 (= G627), E388 (= E629), G406 (= G647), Y407 (≠ W648)
- binding magnesium ion: E207 (= E454), N266 (= N511), E298 (= E540), D328 (= D570)
3qnqD Crystal structure of the transporter chbc, the iic component from the n,n'-diacetylchitobiose-specific phosphotransferase system (see paper)
26% identity, 52% coverage: 12:378/707 of query aligns to 20:420/436 of 3qnqD
3n3tB Crystal structure of putative diguanylate cyclase/phosphodiesterase complex with cyclic di-gmp (see paper)
32% identity, 32% coverage: 428:656/707 of query aligns to 12:248/261 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 (= Q440), L40 (= L456), V41 (≠ L457), R42 (= R458), P53 (≠ G468), N99 (= N511), D161 (= D570), Q185 (≠ R594), E218 (= E626), G219 (= G627), E221 (= E629), G239 (= G647), N240 (≠ W648)
- binding magnesium ion: E38 (= E454), N99 (= N511), E131 (= E540), D161 (= D570), D161 (= D570), D162 (= D571), E218 (= E626)
Q55434 Phytochrome-like protein cph2; Bacteriophytochrome cph2 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
28% identity, 35% coverage: 409:656/707 of query aligns to 596:850/1276 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.
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)
30% identity, 35% coverage: 409:656/707 of query aligns to 161:415/426 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
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)
29% identity, 33% coverage: 428:658/707 of query aligns to 550:786/799 of P76129
- H582 (≠ R460) mutation to A: Loss of cAMP PDE activity.
- H586 (≠ R463) 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.
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)
31% identity, 31% coverage: 437:654/707 of query aligns to 354:576/587 of Q9I0R8
- E464 (= E543) mutation to A: Does not perturb the oligomeric state and does not affect kcat.
4hjfA Eal domain of phosphodiesterase pdea in complex with c-di-gmp and ca++
30% identity, 35% coverage: 419:662/707 of query aligns to 3:255/263 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 (= Q440), L41 (= L456), A42 (≠ L457), R43 (= R458), P54 (≠ G468), L58 (≠ I472), M74 (≠ V488), N100 (= N511), S102 (≠ N513), R186 (= R594), G220 (= G627), E222 (= E629), G240 (= G647), F241 (≠ W648)
- binding calcium ion: E39 (= E454), N100 (= N511), E132 (= E540), D162 (= D570), D162 (= D570), E219 (= E626)
3u2eA Eal domain of phosphodiesterase pdea in complex with 5'-pgpg and mg++
30% identity, 35% coverage: 419:662/707 of query aligns to 1:253/260 of 3u2eA
- binding magnesium ion: E37 (= E454), N98 (= N511), E130 (= E540), D160 (= D570), D160 (= D570), D161 (= D571), E217 (= E626)
- binding : Q23 (= Q440), L39 (= L456), A40 (≠ L457), R41 (= R458), P52 (≠ G468), L56 (≠ I472), M72 (≠ V488), N98 (= N511), S100 (≠ N513), D160 (= D570), D161 (= D571), R184 (= R594), E217 (= E626), E220 (= E629), G238 (= G647), F239 (≠ W648)
5m1tA Pamucr phosphodiesterase, c-di-gmp complex (see paper)
28% identity, 33% coverage: 428:658/707 of query aligns to 9:245/247 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 (= Q440), E35 (= E454), L37 (= L456), R39 (= R458), P50 (≠ G468), L54 (≠ I472), V70 (= V488), N94 (= N511), R180 (= R594), G214 (= G627), E216 (= E629), G234 (= G647), F235 (≠ W648)
- binding magnesium ion: E35 (= E454), N94 (= N511), E126 (= E540), D156 (= D570), D156 (= D570), D157 (= D571), E213 (= E626)
Q8EJM6 Cyclic di-GMP phosphodiesterase PdeB; Phosphodiesterase biofilm protein; EC 3.1.4.52 from Shewanella oneidensis (strain MR-1) (see paper)
29% identity, 33% coverage: 425:657/707 of query aligns to 604:842/856 of Q8EJM6
- E634 (= E454) mutation to A: Lack of activity.
5mfuA Pa3825-eal mn-pgpg structure (see paper)
30% identity, 32% coverage: 428:655/707 of query aligns to 9:242/254 of 5mfuA
- binding guanosine-5'-monophosphate: Q21 (= Q440), L37 (= L456), M38 (≠ L457), R39 (= R458), R49 (≠ E467), P50 (≠ G468), D51 (≠ P469), N94 (= N511), D156 (= D570), D157 (= D571), Q180 (≠ R594), E213 (= E626), G214 (= G627), E216 (= E629), G234 (= G647), Y235 (≠ W648)
- binding manganese (ii) ion: E35 (= E454), N94 (= N511), E126 (≠ D532), D156 (= D570)
5yrpA Crystal structure of the eal domain of mycobacterium smegmatis dcpa (see paper)
28% identity, 32% coverage: 435:660/707 of query aligns to 2:215/224 of 5yrpA
5mf5A Pa3825-eal mg-cdg structure (see paper)
30% identity, 32% coverage: 428:655/707 of query aligns to 9:242/256 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 (= Q440), L37 (= L456), M38 (≠ L457), R39 (= R458), R49 (≠ E467), P50 (≠ G468), D51 (≠ P469), N94 (= N511), Q180 (≠ R594), G214 (= G627), E216 (= E629), G234 (= G647), Y235 (≠ W648), P240 (≠ A653)
- binding magnesium ion: E35 (= E454), V36 (≠ A455), N94 (= N511), N94 (= N511), E126 (≠ D532), D156 (= D570), D157 (= D571), D179 (= D593)
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)
25% identity, 38% coverage: 390:655/707 of query aligns to 108:381/392 of Q9HX69
- Q161 (= Q440) mutation to A: 5.1-fold decrease in kcat.
- E175 (= E454) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- R179 (= R458) mutation to A: 29.1-fold decrease in kcat.
- N233 (= N511) binding ; mutation to A: Loss of activity. Activity can be fully restored at elevated Mg(2+) concentrations (up to 500 mM).
- E265 (= E540) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- T267 (≠ L542) mutation to A: 13.4-fold decrease in kcat.
- E268 (= E543) 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 (= R561) mutation to W: Thermostable. Shows lower enzymatic activity.
- D295 (= D570) binding ; mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- D296 (= D571) mutation to A: 33.5-fold decrease in kcat.
- F297 (= F572) mutation to A: 33.5-fold decrease in kcat.
- S302 (= S577) mutation to A: 4.8-fold decrease in kcat.
- K316 (= K591) mutation to A: Loss of activity. Activity can be partially restored at elevated Mg(2+) concentrations (up to 500 mM).
- D318 (= D593) mutation to A: 8.4-fold decrease in kcat.
- E352 (= E626) mutation E->A,C: Loss of activity.; mutation to D: 30000-fold decrease in kcat.; mutation to Q: 61000-fold decrease in kcat.
- E355 (= E629) mutation to A: 1.3-fold decrease in kcat.
- Q372 (= Q646) mutation to A: 8.4-fold decrease in kcat.
Sites not aligning to the query:
- 56 D→N: 5.2-fold decrease in kcat.
6k6tA Crystal structure of a standalone versatile eal protein from vibrio cholerae o395 - c-di-imp bound form
27% identity, 31% coverage: 431:652/707 of query aligns to 2:221/237 of 6k6tA
- binding 9-[(1R,6R,8R,9S,10R,15S,17R,18S)-3,9,12,18-tetrakis(oxidanyl)-3,12-bis(oxidanylidene)-17-(6-oxidanylidene-3H-purin-9-yl)-2,4,7,11,13,16-hexaoxa-3$l^{5},12$l^{5}-diphosphatricyclo[13.3.0.0^{6,10}]octadecan-8-yl]-3H-purin-6-one: Q11 (= Q440), V28 (≠ L457), R29 (= R458), A36 (≠ G479), I40 (= I489), N75 (= N511), M162 (≠ R594), G196 (= G627), E198 (= E629), G216 (= G647), Y217 (≠ W648)
- binding calcium ion: E25 (= E454), N75 (= N511), E108 (vs. gap), D138 (= D570), D138 (= D570), D139 (= D571), E195 (= E626)
6ih7A Crystal structure of a standalone versatile eal protein from vibrio cholerae o395 - 3',3'-cgamp bound form (see paper)
27% identity, 31% coverage: 431:652/707 of query aligns to 2:221/237 of 6ih7A
- binding 2-amino-9-[(2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-9-(6-amino-9H-purin-9-yl)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecin-2-yl]-1,9-dihydro-6H-purin-6-one: M8 (≠ L437), Q11 (= Q440), L27 (= L456), V28 (≠ L457), R29 (= R458), N75 (= N511), L77 (≠ N513), M162 (≠ R594), G196 (= G627), E198 (= E629), G216 (= G647), Y217 (≠ W648)
- binding calcium ion: E25 (= E454), N75 (= N511), E108 (vs. gap), D138 (= D570), D138 (= D570), D139 (= D571), E195 (= E626)
6ih1A Crystal structure of a standalone versatile eal protein from vibrio cholerae o395 - c-di-gmp bound form (see paper)
27% identity, 31% coverage: 431:652/707 of query aligns to 2:221/237 of 6ih1A
- 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): Q11 (= Q440), L27 (= L456), V28 (≠ L457), R29 (= R458), I40 (= I489), C55 (vs. gap), N75 (= N511), L77 (≠ N513), M162 (≠ R594), G196 (= G627), E198 (= E629), G216 (= G647), Y217 (≠ W648)
- binding calcium ion: E25 (= E454), N75 (= N511), E108 (vs. gap), D138 (= D570), D138 (= D570), D139 (= D571), E195 (= E626)
6ifqB Crystal structure of a standalone versatile eal protein from vibrio cholerae o395 - apo form (see paper)
27% identity, 31% coverage: 431:652/707 of query aligns to 2:221/237 of 6ifqB
Query Sequence
>5208407 FitnessBrowser__PV4:5208407
MAVKDTSSSLFLIAIKESFIALLPFIFVNSLLALIVALVDVWQPSWQGSAAYAWLSQFGR
LLFSFFPLMALLSLSFHFAKYLHVSAVVVASLSIGSQIALHIHGSEAIDLSNGFDFLFGD
ARAIITPILVAYLLQRLMAIKALSLLQSTSLSSYLKLHLNLFIPLILCFVLVTTGIYWVG
ELLGMVLSPLVDSLAASSTLLQLFVRVLATHVLWCFGVHGDIAYMLVLGVDNGLQQVAPN
LTLSQFTDLFVLLGGSGATHSLLIALFIASKDKNAVNVAKLALPFALFNINEILIYGLPI
IFNPRLMLPFVLVPLFNTLIGTLLIVSGWVSFAGNDFAWITPIFLNGYVAGGTLALPLVQ
LLLVCAGVFIYLPFVRRYSLLVGNKGFERDLIKRVQLQQDIEKISERNYARQQSEDLAAN
LNLEKTIKAVLNGELLLYYQPKISLSDRRVVGYEALLRLRNERGQVEGPYFIPAFDQAGY
SNLIDSFVIRRLRDDLQAWAKQGFYPRVSINLNPNSVLSQDVQSMLIELLGDMADRVDIE
VLESMFVADLTAVEASMAYLRQYGFSFVLDDFGTGFSSISLLSKITIDGVKLDRSILENT
GHHKGQVLYRHTCMLCRSLGFNLVAEGVETKAEEAFVASAGVSTVQGWLYAKAMPAAEAK
RYALLQERFSEQAADSRGDSKAELKADVKADVKTEVKAGLKANSKTE
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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