SitesBLAST
Comparing 7024914 FitnessBrowser__ANA3:7024914 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
4gnaA Mouse smp30/gnl-xylitol complex (see paper)
31% identity, 94% coverage: 18:298/300 of query aligns to 13:297/297 of 4gnaA
4gn9A Mouse smp30/gnl-glucose complex (see paper)
31% identity, 94% coverage: 18:298/300 of query aligns to 13:297/297 of 4gn9A
- binding beta-D-glucopyranose: E16 (= E21), G66 (≠ T72), W80 (≠ I86), E81 (= E87), D92 (≠ E98), E93 (≠ S99), R99 (= R105), N101 (= N107), E119 (≠ Q125), Y133 (= Y136), K143 (≠ Q146), N152 (= N155), S168 (= S171), D202 (= D204), Y217 (≠ W219)
- binding calcium ion: E16 (= E21), N152 (= N155), D202 (= D204)
4gn8A Mouse smp30/gnl-1,5-ag complex (see paper)
31% identity, 94% coverage: 18:298/300 of query aligns to 13:297/297 of 4gn8A
- binding 1,5-anhydro-D-glucitol: Q63 (≠ K69), R99 (= R105), N101 (= N107), A108 (≠ Q114), G109 (= G115), E119 (≠ Q125), P122 (≠ T128), N152 (= N155), Y164 (= Y167), A175 (≠ Q178), D179 (= D182), Q181 (≠ E184), R189 (= R192), V191 (vs. gap), D202 (= D204), Y217 (≠ W219), P227 (= P229), Y293 (≠ P294), S294 (≠ R295)
- binding calcium ion: E16 (= E21), N152 (= N155), D202 (= D204)
4gn7A Mouse smp30/gnl (see paper)
31% identity, 94% coverage: 18:298/300 of query aligns to 13:297/297 of 4gn7A
3g4hA Crystal structure of human senescence marker protein-30 (zinc bound) (see paper)
30% identity, 97% coverage: 8:298/300 of query aligns to 3:297/297 of 3g4hA
Q15493 Regucalcin; RC; Gluconolactonase; GNL; Senescence marker protein 30; SMP-30; EC 3.1.1.17 from Homo sapiens (Human) (see 2 papers)
30% identity, 97% coverage: 8:298/300 of query aligns to 5:299/299 of Q15493
- E18 (= E21) binding ; mutation to A: Reduces enzyme activity by about 90%.
- N103 (= N107) mutation to A: Reduces enzyme activity by about 95%.
- N154 (= N155) binding ; mutation to A: Reduces enzyme activity by about 95%.
- D204 (= D204) binding ; mutation to A: Reduces enzyme activity by over 98%.
4gncA Human smp30/gnl-1,5-ag complex (see paper)
30% identity, 97% coverage: 8:298/300 of query aligns to 4:298/298 of 4gncA
- binding 1,5-anhydro-D-glucitol: E17 (= E21), R100 (= R105), N102 (= N107), D203 (= D204), T245 (= T245), N253 (≠ K253), Y254 (≠ R254), G290 (= G290), I291 (≠ V291)
- binding calcium ion: E17 (= E21), D103 (= D108), N153 (= N155), D203 (= D204)
Q9A9Z1 D-xylonolactone lactonase; Xylono-1,5-lactonase; EC 3.1.1.110 from Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) (see paper)
35% identity, 89% coverage: 19:285/300 of query aligns to 15:276/289 of Q9A9Z1
- E17 (= E21) binding
- N145 (= N155) binding
- D195 (= D204) binding
7pldB Caulobacter crescentus xylonolactonase with (r)-4-hydroxy-2- pyrrolidone (see paper)
35% identity, 89% coverage: 19:285/300 of query aligns to 15:276/289 of 7pldB
- binding (R)-4-hydroxy-2-pyrrolidone: L15 (= L19), E17 (= E21), I31 (= I37), A64 (≠ P70), G66 (≠ T72), F67 (≠ L73), P80 (≠ E87), R98 (= R105), N100 (= N107), E119 (≠ R126), D138 (≠ H147), N145 (= N155), K180 (= K191), D195 (= D204), W210 (= W219), W210 (= W219)
- binding fe (ii) ion: E17 (= E21), N145 (= N155), D195 (= D204)
7plbB Caulobacter crescentus xylonolactonase with d-xylose (see paper)
35% identity, 89% coverage: 19:285/300 of query aligns to 15:276/289 of 7plbB
- binding fe (ii) ion: E17 (= E21), N145 (= N155), D195 (= D204)
- binding beta-D-xylopyranose: L15 (= L19), E17 (= E21), E89 (≠ Q96), V90 (≠ P97), D92 (≠ S99), R98 (= R105), N100 (= N107), R109 (= R116), D130 (= D139), N145 (= N155), D174 (≠ Q185), D195 (= D204)
- binding alpha-D-xylopyranose: A64 (≠ P70), G66 (≠ T72), F67 (≠ L73), P80 (≠ E87)
5gx1A Luciferin-regenerating enzyme collected with serial synchrotron rotational crystallography with accumulated dose of 1.1 mgy (1st measurement) (see paper)
31% identity, 91% coverage: 19:290/300 of query aligns to 15:299/307 of 5gx1A
5d9bA Luciferin-regenerating enzyme solved by siras using xfel (refined against native data) (see paper)
31% identity, 91% coverage: 19:290/300 of query aligns to 15:299/307 of 5d9bA
3dr2A Structural and functional analyses of xc5397 from xanthomonas campestris: a gluconolactonase important in glucose secondary metabolic pathways (see paper)
33% identity, 33% coverage: 134:233/300 of query aligns to 167:263/299 of 3dr2A
Sites not aligning to the query:
3o4pA Dfpase at 0.85 angstrom resolution (h atoms included) (see paper)
23% identity, 53% coverage: 107:266/300 of query aligns to 120:292/314 of 3o4pA
- active site: N120 (= N107), N175 (= N155), D229 (= D204), H287 (≠ S261)
- binding calcium ion: N120 (= N107), N175 (= N155), D229 (= D204), D232 (= D207), L273 (≠ I247), H274 (≠ A248)
- binding 1,2-dimethoxyethane: W244 (= W219), K269 (≠ H243)
- binding 2-methoxyethanol: K151 (≠ Q131), A170 (≠ N150), F171 (≠ L151), E194 (≠ D170), K214 (≠ R190)
Sites not aligning to the query:
Q7SIG4 Diisopropyl-fluorophosphatase; DFPase; EC 3.1.8.2 from Loligo vulgaris (Common European squid) (see 4 papers)
23% identity, 53% coverage: 107:266/300 of query aligns to 120:292/314 of Q7SIG4
- N120 (= N107) mutation to D: 96% decrease in activity. 100% decrease in activity; when associated with N-229.
- D121 (= D108) mutation to F: 100% decrease in activity.
- Y144 (vs. gap) mutation to S: 8% increase in activity.
- R146 (= R126) mutation to S: 45% decrease in activity.
- M148 (≠ T128) mutation to A: 26% decrease in activity.
- F173 (≠ I153) 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 (= N155) mutation to D: 98% decrease in activity.
- H181 (vs. gap) mutation to N: 20% decrease in activity.
- T195 (≠ S171) mutation to A: 60% decrease in activity.; mutation to L: 11% decrease in activity.; mutation to V: 3% decrease in activity.
- H219 (≠ F194) mutation to N: 3% increase in activity.
- H224 (= H199) mutation to N: 14% increase in activity.
- D229 (= D204) mutation to N: 100% decrease in activity. Loss of calcium 1 binding. 100% decrease in activity; when associated with D-120.
- D232 (= D207) binding ; mutation to S: 3% increase in activity. 19% decrease in activity; when associated with A-271.
- N237 (≠ G212) mutation to S: 4% decrease in activity.
- W244 (= W219) 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 (≠ Q223) mutation to N: 4% increase in activity.
- S271 (≠ T245) mutation to A: 30% increase in activity. 19% decrease in activity; when associated with S-232.
- N272 (≠ S246) mutation to F: 100% decrease in activity.
- L273 (≠ I247) binding
- H274 (≠ A248) binding ; mutation to N: 85% decrease in activity.
- H287 (≠ S261) active site, Proton acceptor; mutation to A: 90% decrease in activity.; mutation to F: 36% decrease in activity.; mutation to L: 21% decrease in activity.; mutation to N: 97% decrease in activity.; mutation to Q: 54% decrease in activity.; mutation to W: 44% decrease in activity.; mutation to Y: 57% 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.
- 304 Q→F: 50% decrease in activity.; Q→W: 3% decrease in activity.
- 314 F→A: 3% increase in activity.
2gvvA Structure of diisopropyl fluorophosphatase (dfpase) in complex with dicyclopentylphosphoroamidate (dcppa) (see paper)
23% identity, 53% coverage: 107:266/300 of query aligns to 118:290/309 of 2gvvA
- active site: N118 (= N107), N173 (= N155), D227 (= D204), H285 (≠ S261)
- binding calcium ion: N118 (= N107), N173 (= N155), D227 (= D204), D230 (= D207), L271 (≠ I247), H272 (≠ A248)
- binding dicyclopentyl phosphoramidate: N118 (= N107), N173 (= N155), D227 (= D204), W242 (= W219)
Sites not aligning to the query:
Query Sequence
>7024914 FitnessBrowser__ANA3:7024914
MQTVTVGELLMTIPVGNRLGEGVLWDDLHQSIWWTDILSSVIYRFHLASRSLETFPMPHR
VGSFGLTAKPTTLIVAFDIGIAIYDIEDQSLTWLAQPESHFAGNRFNDGRIDRQGRFWAG
TMVEQRDTLQQTAALYCLDEKGHCHQHLTNLEISNGLCWSVDGRTLYHADSPKHQIYQYD
FDIEQGLLSRKRLFASTSHHIFPDGSDVDAAGYLWNAQWGGGQVVRYRPDGEVDLILKLP
VTHPTSIAFGGEKRDLLIVTSAKHSLDASQLDQEPQAGDVFIYPLQGIYGVNSPRFCGQL
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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