SitesBLAST
Comparing Ga0059261_0129 FitnessBrowser__Korea:Ga0059261_0129 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 8 hits to proteins with known functional sites (download)
P0AEY3 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Escherichia coli (strain K12) (see paper)
52% identity, 93% coverage: 20:263/263 of query aligns to 4:259/263 of P0AEY3
- R95 (= R111) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K131) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K180) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KIDEE 180:184) binding
- E171 (= E183) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E184) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E187) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ E196) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ ERAE 196:199) binding
- E192 (= E199) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E200) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D203) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K229) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFEAR 229:233) binding
- R226 (= R233) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W257) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K261) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
3crcA Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
48% identity, 93% coverage: 20:263/263 of query aligns to 3:224/225 of 3crcA
Q9X015 Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG; NTP-PPase; EC 3.6.1.1; EC 3.6.1.9 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
44% identity, 92% coverage: 20:261/263 of query aligns to 8:250/255 of Q9X015
- E41 (= E54) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E55) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E58) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E74) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R110) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R111) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K131) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E187) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ A190) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (= EE 199:200) mutation to AA: Has little effects on the NTPase activity.
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
45% identity, 93% coverage: 20:263/263 of query aligns to 3:218/220 of 3crcB
A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
37% identity, 60% coverage: 12:169/263 of query aligns to 76:238/324 of A0R3C4
- A222 (= A153) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
38% identity, 57% coverage: 21:169/263 of query aligns to 85:235/325 of P96379
- A219 (= A153) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
40% identity, 35% coverage: 21:111/263 of query aligns to 85:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
28% identity, 43% coverage: 20:131/263 of query aligns to 2:113/114 of 2yxhA
Query Sequence
>Ga0059261_0129 FitnessBrowser__Korea:Ga0059261_0129
MSDREAPPAIDIAAIEPPGIERLMAIMARLRDPVTGCEWDTVQTFATIAPYTIEEAYEVA
DAIERHDMADLKDELGDLLLQVIFHSRMAQEAGDFDLSDVIAGICAKMERRHPHIFLGAA
EGGHHLWEQIKAAERGDKGASGALDGVATGLPALLRAEKLQKRAARTGFDWPDPSGARAK
IDEELAEVEAAASDAERAEEIGDLLFAMVNWSRKLGVDPEAALRAANTKFEARFRAMEAE
AGDAFATLDLDAQEALWQQVKRR
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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