SitesBLAST
Comparing 8502372 FitnessBrowser__Miya:8502372 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)
34% identity, 95% coverage: 12:285/287 of query aligns to 2:260/263 of P0AEY3
- R95 (= R104) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K128) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (≠ Q195) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ QVEAE 195:199) binding
- E171 (≠ A198) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E199) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E202) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ R214) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ RQEQ 214:217) binding
- E192 (≠ Q217) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E218) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D221) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K247) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFLRR 247:251) binding
- R226 (= R251) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W278) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K282) 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)
35% identity, 95% coverage: 14:287/287 of query aligns to 8:255/255 of Q9X015
- E41 (= E47) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E48) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E51) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E67) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R103) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R104) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K128) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E202) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ A208) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ QE 217:218) 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)
29% identity, 95% coverage: 12:285/287 of query aligns to 1:225/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
29% identity, 91% coverage: 21:281/287 of query aligns to 3:215/220 of 3crcB
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 61% coverage: 31:205/287 of query aligns to 102:268/325 of P96379
- A219 (≠ Q147) 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)
35% identity, 61% coverage: 31:205/287 of query aligns to 102:271/324 of A0R3C4
- A222 (= A149) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
41% identity, 26% coverage: 31:104/287 of query aligns to 102:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
26% identity, 40% coverage: 14:129/287 of query aligns to 2:114/114 of 2yxhA
Query Sequence
>8502372 FitnessBrowser__Miya:8502372
MSTEPASPNSPHSLQAITDVIDRLLAPEGCPWDREQTPESLADYVIEECFELVEAIRSGK
VHDVREELGDVMFLLAFIGRLYADKGAFTLADAVEGNAAKMIRRHPHVFAEGECASREEL
LRNWERIKREEKAAAMAEDADAEGEAQAAPAEGAQKGVFDSLPKGLPPLVKAYRLHSKAA
RVDFTWESDEDVEQQVEAEWLEWLDASASGDKERQEQELGDFLFTIVELGRRKGIKANAA
LDYATLKFLRRFEGMEALARERGLDFPNLPFEGKDALWNEVKAAEKA
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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