SitesBLAST
Comparing WP_057508176.1 NCBI__GCF_001431535.1:WP_057508176.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
53% identity, 96% coverage: 8:270/273 of query aligns to 2:260/263 of P0AEY3
- R95 (= R101) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K125) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K176) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KAAEE 176:180) binding
- 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 ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ R199) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ RLQE 199:202) binding
- E192 (= E202) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E203) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D206) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K232) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (= KFERR 232:236) binding
- R226 (= R236) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W263) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K267) 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, 95% coverage: 8:266/273 of query aligns to 1:221/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
44% identity, 95% coverage: 8:266/273 of query aligns to 1:215/220 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)
41% identity, 95% coverage: 13:272/273 of query aligns to 11:255/255 of Q9X015
- E41 (= E44) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E45) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E48) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E64) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R100) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R101) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K125) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ R190) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ V193) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (= EE 202:203) 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)
38% identity, 56% coverage: 14:165/273 of query aligns to 91:235/325 of P96379
- A219 (≠ E149) 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, 56% coverage: 14:165/273 of query aligns to 91:238/324 of A0R3C4
- A222 (≠ E149) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
43% identity, 32% coverage: 14:101/273 of query aligns to 91:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
30% identity, 35% coverage: 12:106/273 of query aligns to 4:95/114 of 2yxhA
Query Sequence
>WP_057508176.1 NCBI__GCF_001431535.1:WP_057508176.1
MSTSDAATELGRLLAIMARLRDPQGGCPWDLEQDFSSIAPYTIEEAYEVADAIDRGDLDD
LCDELGDLLLQVVFHAQMAQEQGAFAFADVARSINDKMVRRHPHIFADASAGDAAEVLRN
WDAIKREERAAKGETDASALAGISRGLPEWQRAMKLQSRAAKVGFDWPGPLPVLDKAAEE
LQELREEFERGDVAANKARLQEELGDLLFVCANLARHAELDLGAALRGANHKFERRFRAM
EARAGEHGTRLAELDLDAQEALWQHAKAAESAS
Or try a new SitesBLAST search
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