SitesBLAST
Comparing WP_035238726.1 NCBI__GCF_000745975.1:WP_035238726.1 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)
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)
42% identity, 95% coverage: 7:256/264 of query aligns to 11:250/255 of Q9X015
- E41 (= E37) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E38) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E41) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E57) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R93) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R94) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K118) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ N179) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ L182) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ LE 191:192) mutation to AA: Has little effects on the NTPase activity.
P0AEY3 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Escherichia coli (strain K12) (see paper)
38% identity, 97% coverage: 1:257/264 of query aligns to 1:258/263 of P0AEY3
- R95 (= R94) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K118) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (≠ T170) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ TAVSE 170:174) binding
- E171 (≠ S173) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E174) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E177) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ D188) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ DAML 188:191) binding
- E192 (≠ L191) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E192) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D195) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K221) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFEQR 221:225) binding
- R226 (= R225) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W252) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K256) 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)
34% identity, 92% coverage: 7:248/264 of query aligns to 6:216/225 of 3crcA
Sites not aligning to the query:
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
32% identity, 93% coverage: 7:252/264 of query aligns to 6:212/220 of 3crcB
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 54% coverage: 17:159/264 of query aligns to 98:235/325 of P96379
- A219 (≠ G143) 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)
34% identity, 74% coverage: 2:197/264 of query aligns to 85:273/324 of A0R3C4
- A222 (≠ G143) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
32% identity, 39% coverage: 7:109/264 of query aligns to 5:105/114 of 2yxhA
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
36% identity, 30% coverage: 17:94/264 of query aligns to 98:173/177 of 7yh5B
Query Sequence
>WP_035238726.1 NCBI__GCF_000745975.1:WP_035238726.1
METIIPLLEIIRRLRGKNGCAWDRKQTPSSMWKCLAEELYELEEAIVKDDEDNIIEELGD
VLFQILFIMEIYADAGRFSFERVVNTVAEKMIRRHPHVYGDSRITSEDGLNKQWEAIKAG
EKAGSGISERRSALDNVPGGMPGLLRALKVSKSAVKAGFEWDNLNQVLDTAVSEIHEFNA
ALSMDQDDAMLEFGDILFSLVNVARFAGFHPETALYRSTSKFEQRFRIMEAALEKQGLDL
KQMPSEEKEKHWLKAKQVYAQKKA
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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