SitesBLAST
Comparing 3607751 FitnessBrowser__Dino:3607751 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)
54% identity, 91% coverage: 23:275/279 of query aligns to 4:257/263 of P0AEY3
- R95 (= R114) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K139) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K188) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KLAEE 188:192) binding
- E171 (= E191) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E192) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E195) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (= K207) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ KLHE 207:210) binding
- E192 (= E210) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E211) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D214) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K240) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFTRR 240:244) binding
- R226 (= R244) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W271) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K275) 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, 90% coverage: 23:272/279 of query aligns to 3:219/225 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)
43% identity, 90% coverage: 26:276/279 of query aligns to 11:251/255 of Q9X015
- E41 (= E57) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E58) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E61) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E77) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (≠ D113) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R114) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K139) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E195) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ D198) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (= EE 210:211) 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)
44% identity, 90% coverage: 23:272/279 of query aligns to 3:213/220 of 3crcB
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 53% coverage: 29:177/279 of query aligns to 93:235/325 of P96379
- A219 (= A161) 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, 53% coverage: 29:177/279 of query aligns to 93:238/324 of A0R3C4
- A222 (= A161) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
39% identity, 31% coverage: 29:114/279 of query aligns to 93:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 42% coverage: 23:139/279 of query aligns to 2:113/114 of 2yxhA
Query Sequence
>3607751 FitnessBrowser__Dino:3607751
MTRAKTRDRADSDTLCHDPEGGLPRLLEIMRRLRDPETGCPWDVEQTFETIAPYTIEEAY
EVSDAIDRGDWADLKSELGDLLLQTVYQTQIGAERGLFDFHDVANGIAQKMLDRHPHVFG
DESNAKSAEQQTRDWEAQKARERAAKAEKGVLDGVALGLPALMRALKLQKRAARVGFDWD
DADQVLAKLAEESAELADARDAGDAAKLHEEFGDLLFVVVNLGRHLGLDPEHALRDANAK
FTRRFAHIEAELARAGRNPEAASLDEMEALWQAAKANGL
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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