SitesBLAST
Comparing Synpcc7942_1493 FitnessBrowser__SynE:Synpcc7942_1493 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)
43% identity, 90% coverage: 23:273/279 of query aligns to 6:259/263 of P0AEY3
- R95 (= R112) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K136) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K187) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KFEEE 187:191) binding
- E171 (= E190) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E191) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E194) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (vs. gap) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ --EA 208:209) binding
- E192 (≠ A209) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E210) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D213) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (≠ R239) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ RFVAR 239:243) binding
- R226 (= R243) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W267) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K271) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
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, 89% coverage: 23:271/279 of query aligns to 10:250/255 of Q9X015
- E41 (= E55) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E56) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E59) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E75) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R111) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R112) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K136) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E194) mutation to A: Has little effects on the NTPase activity.
- E176 (= E197) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ AE 209:210) mutation to AA: Has little effects on the NTPase activity.
3crcA Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
38% identity, 90% coverage: 23:273/279 of query aligns to 5:224/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
36% identity, 84% coverage: 40:273/279 of query aligns to 14:218/220 of 3crcB
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
42% identity, 55% coverage: 23:176/279 of query aligns to 86:235/325 of P96379
- A219 (≠ P160) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
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, 56% coverage: 21:176/279 of query aligns to 87:238/324 of A0R3C4
- A222 (≠ P160) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
45% identity, 32% coverage: 23:112/279 of query aligns to 86:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 30% coverage: 36:119/279 of query aligns to 14:97/114 of 2yxhA
Query Sequence
>Synpcc7942_1493 FitnessBrowser__SynE:Synpcc7942_1493
MGVDFSESVPAPNQDAIATALLQLVAVVAQLRDPEQGCPWDREQTPTSLIPYVLEEAYEV
VHALRQGNPNAIAEELGDLLLQVVLQAQIASESQQFDLATVADGITEKLIRRHPHVFGEA
IAETPEAVQATWQAIKAREKGEVAETLTHCLSRYAATLPPLTAALKISQRAAKAGFEWPN
LAGVWDKFEEELAELKEALDSGDRDHAEAELGDLLFSLVNIARWCQLDPVAALQGTNDRF
VARFQKVEAAAGQSLDSLGIETLEKLWQQAKRELGQSSV
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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