SitesBLAST
Comparing WP_012503182.1 NCBI__GCF_000020505.1:WP_012503182.1 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)
47% identity, 89% coverage: 28:269/271 of query aligns to 8:250/255 of Q9X015
- E41 (= E59) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E60) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E63) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E79) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (≠ S115) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R116) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K140) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E192) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ H195) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (= EE 204:205) 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)
40% identity, 90% coverage: 27:271/271 of query aligns to 3:259/263 of P0AEY3
- R95 (= R116) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K140) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K185) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KLTEE 185:189) binding
- E171 (= E188) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E189) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E192) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ E201) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ EREE 201:204) binding
- E192 (= E204) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E205) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D208) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K234) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (≠ KFMDR 234:238) binding
- R226 (= R238) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W265) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K269) 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)
36% identity, 90% coverage: 27:271/271 of query aligns to 2:224/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
36% identity, 84% coverage: 44:271/271 of query aligns to 14:218/220 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)
34% identity, 88% coverage: 24:262/271 of query aligns to 83:294/324 of A0R3C4
- A222 (≠ E158) 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)
30% identity, 88% coverage: 25:262/271 of query aligns to 81:291/325 of P96379
- A219 (≠ E158) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
40% identity, 34% coverage: 25:116/271 of query aligns to 81:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
25% identity, 38% coverage: 28:131/271 of query aligns to 2:105/114 of 2yxhA
Query Sequence
>WP_012503182.1 NCBI__GCF_000020505.1:WP_012503182.1
MKHEANPSIEILKESVLNHNAVTPAEHFERVVNLVRVLRSECPWDRKQTPESLAHLLLEE
SYELVHAIDTGDDPELKKELGDLFLHVCFQVLLADEAGKFSFVDVFEALCHKLISRHPHV
FGDVKADTEQAVLGNWENLKMKEGRKSLLEGVPNAMSELLRAYRVQKKVAGVGFDWPSDE
GVLDKLTEEIGELRHAADKSEREEEFGDLLFTIVNYSRFIDTNPEDALRKATNKFMDRFR
KVEESVQASGKSWQEFSAEELDSLWNEAKKS
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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