SitesBLAST
Comparing WP_017598043.1 NCBI__GCF_000341125.1:WP_017598043.1 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)
A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
40% identity, 88% coverage: 24:262/271 of query aligns to 81:310/324 of A0R3C4
- A222 (= A176) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
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)
36% identity, 88% coverage: 27:265/271 of query aligns to 5:249/255 of Q9X015
- E41 (≠ Q61) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E62) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E65) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E81) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R122) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R123) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K147) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (vs. gap) mutation to A: Has little effects on the NTPase activity.
- E176 (vs. gap) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (≠ GG 201:202) mutation to AA: Has little effects on the NTPase activity.
P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 90% coverage: 27:271/271 of query aligns to 84:316/325 of P96379
- A219 (= A176) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
P0AEY3 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Escherichia coli (strain K12) (see paper)
35% identity, 81% coverage: 28:247/271 of query aligns to 2:238/263 of P0AEY3
- R95 (= R123) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K147) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (≠ G191) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ GVPAD 191:195) binding
- E171 (≠ A194) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (≠ D195) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (vs. gap) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ G202) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ G--- 202) binding
- E192 (vs. gap) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (vs. gap) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (≠ G205) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (≠ R231) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ RFDAR 231:235) binding
- R226 (= R235) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
Sites not aligning to the query:
- 253 binding ; W→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- 257 K→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, 86% coverage: 28:260/271 of query aligns to 1:220/225 of 3crcA
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
46% identity, 36% coverage: 27:123/271 of query aligns to 84:177/177 of 7yh5B
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
32% identity, 81% coverage: 28:247/271 of query aligns to 1:197/220 of 3crcB
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 38% coverage: 32:134/271 of query aligns to 4:101/114 of 2yxhA
Query Sequence
>WP_017598043.1 NCBI__GCF_000341125.1:WP_017598043.1
MHETRDGGGHHGGPGEARSGDAGPAPGHRLPRLVEVMATLRRECPWDRGQTHESLAKYLI
QEAYETLEIIEEGDPSLLPEELGDVLLQVVFHAAIAAERPEGDPARFTVDDVADAIIDKM
TRRHPHVFGGVEVSGADEVKSNWEAIKAAERREKARARGHEGEGSVLDGVPFAQPAVLLS
EELQRRAVRNGVPADLVVDDGGAGGELFAAVATERERGRDAEGDLRAAARRFDARVRAAE
ALAGADGRDPRELSEAEWRRYWHRAGDVQEG
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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