SitesBLAST
Comparing 353876 FitnessBrowser__Btheta:353876 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)
41% identity, 96% coverage: 9:260/262 of query aligns to 1:259/263 of P0AEY3
- R95 (= R100) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K124) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K171) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KVKEE 171:175) binding
- E171 (= E174) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E175) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E178) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (= K190) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ KAEA 190:193) binding
- E192 (≠ A193) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E194) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D197) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K223) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFIRR 223:227) binding
- R226 (= R227) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W254) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K258) 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)
42% identity, 94% coverage: 12:258/262 of query aligns to 8:250/255 of Q9X015
- E41 (= E43) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E44) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E47) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E63) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (≠ F99) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R100) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K124) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ V181) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ A184) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ AE 193:194) 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, 94% coverage: 14:260/262 of query aligns to 5:224/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
35% identity, 94% coverage: 14:260/262 of query aligns to 5:218/220 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)
36% identity, 56% coverage: 18:163/262 of query aligns to 93:241/324 of A0R3C4
- A222 (≠ S144) 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)
37% identity, 55% coverage: 18:160/262 of query aligns to 93:235/325 of P96379
- A219 (≠ S144) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
44% identity, 31% coverage: 18:97/262 of query aligns to 93:174/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
28% identity, 37% coverage: 14:109/262 of query aligns to 4:99/114 of 2yxhA
Query Sequence
>353876 FitnessBrowser__Btheta:353876
MIHTREEQMEAFGRFLDILDELRVKCPWDRKQTNESLRPNTIEETYELCDALMRDDKKDI
CKELGDVLLHVAFYAKIGSETGDFDIKDVCDKLCDKLIFRHPHVFGEVKAETAGQVSENW
EQLKLKEKDGNKSVLSGVPSALPSLIKAYRIQDKARNVGFDWEEREQVWDKVKEEIREFQ
VEVANMDKEKAEAEFGDVMFSLINAARLYKINPDNALELTNQKFIRRFNYLEEHTIKEGK
NLKDMSLEEMDAIWNEAKRKGL
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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