SitesBLAST
Comparing CCNA_01821 FitnessBrowser__Caulo:CCNA_01821 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)
55% identity, 92% coverage: 21:272/275 of query aligns to 7:260/263 of P0AEY3
- R95 (= R109) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K133) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K182) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KLREE 182:186) binding
- E171 (= E185) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E186) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E189) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (= K201) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ KARE 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 (≠ KFTRR 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)
50% identity, 89% coverage: 21:266/275 of query aligns to 6:219/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
46% identity, 89% coverage: 21:266/275 of query aligns to 6:213/220 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)
42% identity, 92% coverage: 21:273/275 of query aligns to 11:254/255 of Q9X015
- E41 (= E52) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E53) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E56) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E72) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R108) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R109) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K133) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ V192) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ A195) 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.
A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
43% identity, 55% coverage: 22:171/275 of query aligns to 91:238/324 of A0R3C4
- A222 (= A155) 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)
42% identity, 59% coverage: 9:171/275 of query aligns to 78:235/325 of P96379
- A219 (= A155) 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, 37% coverage: 9:109/275 of query aligns to 78:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 30% coverage: 35:117/275 of query aligns to 16:98/114 of 2yxhA
Query Sequence
>CCNA_01821 FitnessBrowser__Caulo:CCNA_01821
MSPQTPPLAPPSDDQHPLFALIEIMAKLRDPNGGCPWDLEQTFATIAPYTVEEAYEVADA
IERGDLSDLKEELGDLLLQVVFHSRMAQEQGAFDIADVARAISDKMIRRHPHVFGDHAYE
DLSAQVAGWEQLKAQERQAKAKTGVLDDVPTGLPALTRAVKLTKRAARVGFDWPTANEVL
DKLREETDEIAVEIAAGDLAKAREELGDILFVCANLARKLDVDPEDALRATNAKFTRRFG
FVETELAKRGKTPDQSDLAEMDGLWNDAKAAEKKV
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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