SitesBLAST
Comparing 6936852 FitnessBrowser__SB2B:6936852 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)
57% identity, 93% coverage: 15:271/275 of query aligns to 4:260/263 of P0AEY3
- R95 (= R106) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K130) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K179) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KVEEE 179:183) binding
- E171 (= E182) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E183) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E186) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ R200) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ RVAS 200:203) binding
- E192 (≠ S203) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E204) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D207) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K233) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (= KFERR 233:237) binding
- R226 (= R237) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W264) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K268) 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)
51% identity, 93% coverage: 15:271/275 of query aligns to 3:225/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
48% identity, 93% coverage: 15:271/275 of query aligns to 3:219/220 of 3crcB
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)
41% identity, 91% coverage: 18:268/275 of query aligns to 11:250/255 of Q9X015
- E41 (= E49) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E50) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E53) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E69) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (≠ S105) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R106) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K130) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ V191) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ D194) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ SE 203:204) mutation to AA: Has little effects on the NTPase activity.
A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
36% identity, 55% coverage: 19:168/275 of query aligns to 91:238/324 of A0R3C4
- A222 (= A152) 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)
34% identity, 67% coverage: 19:202/275 of query aligns to 91:262/325 of P96379
- A219 (= A152) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
36% identity, 32% coverage: 19:106/275 of query aligns to 91:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
26% identity, 31% coverage: 32:117/275 of query aligns to 16:101/114 of 2yxhA
Query Sequence
>6936852 FitnessBrowser__SB2B:6936852
MSTEIIANEEPNADINPLLAIMAKLRDPKHGCPWDKAQRFETIVPFTLEEAYEVADTIER
MDLDELPDELGDLLFQVVFYCQLGKEQGLFDFDEVVKRICAKLTSRHPHVFGDIEVSSSK
EVKDNWEAIKASERKAKDKHSVLDDVPVGLPALSRAAKIQKRVARVGFDWGELPPVVAKV
EEEIAEVLAEVQVDSPDQERVASEMGDLLFAVVNMARHLGVEPEQALRRANQKFERRFRG
VEELATLGGRQLTDYSLAELDGFWDQVKEQEKSPR
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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