SitesBLAST
Comparing GFF2160 FitnessBrowser__WCS417:GFF2160 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
7pldB Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
34% identity, 96% coverage: 10:284/287 of query aligns to 12:285/289 of 7pldB
- binding (R)-4-hydroxy-2-pyrrolidone: L15 (= L13), E17 (= E15), I31 (= I31), A64 (≠ G62), G66 (≠ A64), F67 (≠ L65), P80 (≠ L77), R98 (= R95), N100 (= N97), E119 (= E118), D138 (≠ L145), N145 (= N152), K180 (≠ A187), D195 (= D200), W210 (= W215), W210 (= W215)
- binding fe (ii) ion: E17 (= E15), N145 (= N152), D195 (= D200)
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
34% identity, 96% coverage: 10:284/287 of query aligns to 12:285/289 of 7plbB
- binding fe (ii) ion: E17 (= E15), N145 (= N152), D195 (= D200)
- binding beta-D-xylopyranose: L15 (= L13), E17 (= E15), E89 (≠ C86), V90 (= V87), D92 (= D89), R98 (= R95), N100 (= N97), R109 (= R106), D130 (= D136), N145 (= N152), D174 (= D181), D195 (= D200)
- binding alpha-D-xylopyranose: A64 (≠ G62), G66 (≠ A64), F67 (≠ L65), P80 (≠ L77)
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
34% identity, 96% coverage: 10:284/287 of query aligns to 12:285/289 of Q9A9Z1
- E17 (= E15) binding
- N145 (= N152) binding
- D195 (= D200) binding
Q15493 Regucalcin; RC; Gluconolactonase; GNL; Senescence marker protein 30; SMP-30; EC 3.1.1.17 from Homo sapiens (Human) (see 2 papers)
29% identity, 90% coverage: 6:263/287 of query aligns to 9:268/299 of Q15493
- E18 (= E15) binding ; mutation to A: Reduces enzyme activity by about 90%.
- N103 (= N97) mutation to A: Reduces enzyme activity by about 95%.
- N154 (= N152) binding ; mutation to A: Reduces enzyme activity by about 95%.
- D204 (= D200) binding ; mutation to A: Reduces enzyme activity by over 98%.
3g4hA Crystal structure of human senescence marker protein-30 (zinc bound) (see paper)
29% identity, 90% coverage: 6:263/287 of query aligns to 7:266/297 of 3g4hA
4gncA Human smp30/gnl-1,5-ag complex (see paper)
29% identity, 90% coverage: 6:263/287 of query aligns to 8:267/298 of 4gncA
- binding 1,5-anhydro-D-glucitol: E17 (= E15), R100 (= R95), N102 (= N97), D203 (= D200), T245 (= T241), N253 (= N249), Y254 (≠ L250)
- binding calcium ion: E17 (= E15), D103 (≠ E98), N153 (= N152), D203 (= D200)
Sites not aligning to the query:
5gx1A Luciferin-regenerating enzyme collected with serial synchrotron rotational crystallography with accumulated dose of 1.1 mgy (1st measurement) (see paper)
31% identity, 89% coverage: 10:263/287 of query aligns to 12:276/307 of 5gx1A
5d9bA Luciferin-regenerating enzyme solved by siras using xfel (refined against native data) (see paper)
31% identity, 89% coverage: 10:263/287 of query aligns to 12:276/307 of 5d9bA
4gnaA Mouse smp30/gnl-xylitol complex (see paper)
27% identity, 92% coverage: 1:263/287 of query aligns to 4:266/297 of 4gnaA
4gn9A Mouse smp30/gnl-glucose complex (see paper)
27% identity, 92% coverage: 1:263/287 of query aligns to 4:266/297 of 4gn9A
- binding beta-D-glucopyranose: E16 (= E15), G66 (≠ D63), W80 (≠ L77), E81 (≠ A78), D92 (= D89), E93 (≠ P90), R99 (= R95), N101 (= N97), E119 (≠ Q119), Y133 (≠ F133), K143 (≠ P143), N152 (= N152), S168 (= S168), D202 (= D200), Y217 (≠ W215)
- binding calcium ion: E16 (= E15), N152 (= N152), D202 (= D200)
4gn8A Mouse smp30/gnl-1,5-ag complex (see paper)
27% identity, 92% coverage: 1:263/287 of query aligns to 4:266/297 of 4gn8A
- binding 1,5-anhydro-D-glucitol: Q63 (≠ E60), R99 (= R95), N101 (= N97), A108 (≠ S104), G109 (= G105), E119 (≠ Q119), P122 (≠ D122), N152 (= N152), Y164 (≠ H164), A175 (vs. gap), D179 (≠ A177), Q181 (= Q179), R189 (≠ Q188), V191 (≠ W190), D202 (= D200), Y217 (≠ W215), P227 (= P225)
- binding calcium ion: E16 (= E15), N152 (= N152), D202 (= D200)
Sites not aligning to the query:
4gn7A Mouse smp30/gnl (see paper)
27% identity, 92% coverage: 1:263/287 of query aligns to 4:266/297 of 4gn7A
2gvvA Structure of diisopropyl fluorophosphatase (dfpase) in complex with dicyclopentylphosphoroamidate (dcppa) (see paper)
21% identity, 56% coverage: 97:257/287 of query aligns to 118:284/309 of 2gvvA
- active site: N118 (= N97), N173 (= N152), D227 (= D200)
- binding calcium ion: N118 (= N97), N173 (= N152), D227 (= D200), D230 (≠ A203), L271 (≠ C243), H272 (≠ V244)
- binding dicyclopentyl phosphoramidate: N118 (= N97), N173 (= N152), D227 (= D200), W242 (= W215)
Sites not aligning to the query:
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
21% identity, 56% coverage: 97:257/287 of query aligns to 120:286/314 of 3o4pA
- active site: N120 (= N97), N175 (= N152), D229 (= D200)
- binding calcium ion: N120 (= N97), N175 (= N152), D229 (= D200), D232 (≠ A203), L273 (≠ C243), H274 (≠ V244)
- binding 1,2-dimethoxyethane: W244 (= W215), K269 (≠ R239)
- binding 2-methoxyethanol: K151 (≠ R128), A170 (≠ G147), F171 (≠ L148), E194 (≠ D167), K214 (≠ A187)
Sites not aligning to the query:
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.1.8.2 from Loligo vulgaris (Common European squid) (see 4 papers)
21% identity, 56% coverage: 97:257/287 of query aligns to 120:286/314 of Q7SIG4
- N120 (= N97) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (≠ E98) mutation to F: 100% decrease in activity.
- Y144 (≠ E121) mutation to S: 8% increase in activity.
- R146 (≠ L123) mutation to S: 45% decrease in activity.
- M148 (≠ I125) mutation to A: 26% decrease in activity.
- F173 (≠ I150) mutation to A: 84% decrease in activity.; mutation to L: 28% decrease in activity.; mutation to S: 68% decrease in activity.; mutation to V: 46% decrease in activity.; mutation to W: 19% decrease in activity.; mutation to Y: 53% decrease in activity.
- N175 (= N152) mutation to D: 98% decrease in activity.
- H181 (≠ W156) mutation to N: 20% decrease in activity.
- T195 (≠ S168) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (vs. gap) mutation to N: 3% increase in activity.
- H224 (= H194) mutation to N: 14% increase in activity.
- D229 (= D200) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (≠ A203) binding ; mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G208) mutation to S: 4% decrease in activity.
- W244 (= W215) mutation to F: 44% decrease in activity.; mutation to H: 27% decrease in activity.; mutation to L: 62% decrease in activity.; mutation to Y: No effect on activity.
- H248 (≠ C219) mutation to N: 4% increase in activity.
- S271 (≠ T241) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (≠ S242) mutation to F: 100% decrease in activity.
- L273 (≠ C243) binding
- H274 (≠ V244) binding ; mutation to N: 85% decrease in activity.
Sites not aligning to the query:
- 21 E→Q: 100% decrease in activity. Loss of calcium 1 binding.
- 37 E→Q: 50% decrease in activity.
- 77 Q→F: 100% decrease in activity.; Q→W: No effect on activity.; Q→Y: 6% increase in activity.
- 287 active site, Proton acceptor; H→A: 90% decrease in activity.; H→F: 36% decrease in activity.; H→L: 21% decrease in activity.; H→N: 97% decrease in activity.; H→Q: 54% decrease in activity.; H→W: 44% decrease in activity.; H→Y: 57% decrease in activity.
- 304 Q→F: 50% decrease in activity.; Q→W: 3% decrease in activity.
- 314 F→A: 3% increase in activity.
Query Sequence
>GFF2160 FitnessBrowser__WCS417:GFF2160
MSCIAVTPHRAQLGEGPFWDAPTQALYWVNIAGKQALRLMGGQLQVWQLPEHVSAFIPCE
SGDALVTLSSGVYRLDLATEALTLLCVADPQPGNRGNEARCDASGRLWLGTMQNNIGEQG
EDLPITRRSGGLFRIDADAQVTPLLSGLGIPNTLLWSDDGRHVHFGDSLDGTLYRHAIQP
DGQLDPAQTWFGPHERGGPDGSAMDVDGYIWNARWDGSCLLRLTPDGEVDRIVELPVSRP
TSCVLGGPNLTTLYITSAASPLDHPLDGAVLAMEVDVPGKPCHRFAG
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