SitesBLAST
Comparing WP_013818507.1 NCBI__GCF_000214665.1:WP_013818507.1 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)
50% identity, 96% coverage: 3:262/272 of query aligns to 1:258/263 of P0AEY3
- R95 (= R97) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K121) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K174) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KVEEE 174:178) binding ATP
- E171 (= E177) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E178) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E181) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ H193) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ HVQE 193:196) binding ATP
- E192 (= E196) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E197) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D200) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K226) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFTRR 226:230) binding ATP
- R226 (= R230) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W257) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K261) 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)
47% identity, 93% coverage: 9:262/272 of query aligns to 6:223/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
44% identity, 93% coverage: 9:262/272 of query aligns to 6:217/220 of 3crcB
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)
45% identity, 93% coverage: 8:261/272 of query aligns to 10:250/255 of Q9X015
- E41 (= E40) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E41) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E44) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E60) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (≠ S96) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R97) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K121) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E181) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ Q187) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (= EE 196:197) mutation to AA: Has little effects on the NTPase activity.
A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
39% identity, 57% coverage: 10:163/272 of query aligns to 91:238/324 of A0R3C4
- A222 (= A147) 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)
39% identity, 57% coverage: 10:163/272 of query aligns to 91:235/325 of P96379
- A219 (= A147) 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, 32% coverage: 10:97/272 of query aligns to 91:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
30% identity, 29% coverage: 23:102/272 of query aligns to 16:95/114 of 2yxhA
Query Sequence
>WP_013818507.1 NCBI__GCF_000214665.1:WP_013818507.1
MSLDKTRELLTLMARLRDPETGCAWDVKQDFVSLIPYTIEEAYEVADAIERNDFDDLRGE
LGDLLLQVVFHSRIAEERGLFDFEQVAAGISEKLVSRHPHVFAGVNFETDEQRQQAWDDA
KAQERQQKNTGNKPESVLSGVAKSLPALVACEKIQNRAASHGFDWPDVDPVFDKVEEELQ
EVHEAWQSGDQAHVQEEVGDLLLVVVNLARHLKVNPEIALKEATKKFTRRFNYIEKQIEA
SGRQLRECELAELDGLWHEAKRVQKNPRSGTQ
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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