SitesBLAST
Comparing WP_013257777.1 NCBI__GCF_000143965.1:WP_013257777.1 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)
44% identity, 90% coverage: 17:260/272 of query aligns to 6:257/263 of P0AEY3
- R95 (= R105) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K129) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K176) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KVAEE 176:180) binding ATP
- E171 (= E179) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E180) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E183) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ Q192) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ QREA 192:195) binding ATP
- E192 (≠ A195) 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 ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (≠ R225) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ RFQRR 225:229) binding ATP
- R226 (= R229) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W256) binding ATP; 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)
40% identity, 93% coverage: 11:262/272 of query aligns to 4:252/255 of Q9X015
- E41 (= E48) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E49) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E52) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E68) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R104) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R105) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K129) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E183) 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 (≠ AE 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)
39% identity, 89% coverage: 17:259/272 of query aligns to 5:221/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
37% identity, 89% coverage: 17:259/272 of query aligns to 5:215/220 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, 54% coverage: 19:165/272 of query aligns to 91:238/324 of A0R3C4
- A222 (= A149) 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)
31% identity, 86% coverage: 19:252/272 of query aligns to 91:295/325 of P96379
- A219 (= A149) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
43% identity, 25% coverage: 19:87/272 of query aligns to 91:157/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
25% identity, 39% coverage: 26:130/272 of query aligns to 11:114/114 of 2yxhA
Query Sequence
>WP_013257777.1 NCBI__GCF_000143965.1:WP_013257777.1
MSDQHQQAALAGASFARLVALAARLRAPDGCPWDRQQTVQSSTPYILEEAYEAVDALESG
DRREAMGELGDLLFQVVFQSQLAAEAGDFDARAVIEAVEAKMIRRHPHVFGQERAADAEA
VLRRWSEIKRDERGASQGLLDSVPKGSAALTRAQRLGQKAARVGFDWRGQADVLAKVAEE
AAELTASADAAQREAEFGDLLFALAQWARHGKIDAEAALRRACERFQRRFELMEAAAAGR
GVSLDRLDEAALDELWREAKAALAARQGVGGK
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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