SitesBLAST
Comparing 206625 MicrobesOnline__882:206625 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)
37% identity, 96% coverage: 7:263/267 of query aligns to 3:260/263 of P0AEY3
- R95 (= R98) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K122) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (≠ D169) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ DVERQ 169:173) binding
- E171 (≠ R172) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (≠ Q173) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (≠ A176) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ A192) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ AQEN 192:195) binding
- E192 (≠ N195) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E196) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D199) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K225) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFLRR 225:229) binding
- R226 (= R229) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W256) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K260) 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)
39% identity, 94% coverage: 11:262/267 of query aligns to 11:252/255 of Q9X015
- E41 (= E41) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E42) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E45) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E61) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R97) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R98) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K122) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ D183) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ A186) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ NE 195:196) 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)
32% identity, 96% coverage: 7:263/267 of query aligns to 2:225/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
31% identity, 93% coverage: 15:263/267 of query aligns to 3:219/220 of 3crcB
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 52% coverage: 25:162/267 of query aligns to 102:235/325 of P96379
- A219 (≠ P146) 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, 52% coverage: 25:162/267 of query aligns to 102:238/324 of A0R3C4
- A222 (≠ P146) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
46% identity, 24% coverage: 25:87/267 of query aligns to 102:166/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
28% identity, 35% coverage: 10:103/267 of query aligns to 4:95/114 of 2yxhA
Query Sequence
>206625 MicrobesOnline__882:206625
MTKDNASLARLTDVIDRLLAPEGCPWDKEQTPESLCDYLVEECFELVEAIRSGNADEVRE
EMGDVMFLLAFLGRLYADKGAFTLDDAMANNAAKMIRRHPHVFSDTTYADRDEFLRNWES
IKRAEKADAEGEPQGVYDSLPASLPPLLKAYRIHSKAARVGFTWPEDEDVERQVEAEWLE
LLDVLAGDDKAAQENELGDLIFSLVELGRRKGIKANTALDMTNLKFLRRFRRMEALARER
GLDFPALSLDDKDELWNEAKAAEAAAR
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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