SitesBLAST
Comparing WP_013983285.1 NCBI__GCF_000013785.1:WP_013983285.1 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)
P0AEY3 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Escherichia coli (strain K12) (see paper)
54% identity, 98% coverage: 1:270/276 of query aligns to 1:260/263 of P0AEY3
- R95 (= R95) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K127) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K180) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KVREE 180:184) binding ATP
- E171 (= E183) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E184) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E187) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (≠ A199) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (≠ AIAE 199:202) binding ATP
- 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 ATP; 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 ATP
- R226 (= R236) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W263) binding ATP; 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, 97% coverage: 3:270/276 of query aligns to 2:225/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
44% identity, 97% coverage: 3:270/276 of query aligns to 2:219/220 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)
39% identity, 97% coverage: 6:272/276 of query aligns to 10:255/255 of Q9X015
- E41 (= E38) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
- E42 (= E39) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
- E45 (= E42) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- E61 (= E58) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
- R97 (= R94) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
- R98 (= R95) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
- K118 (= K127) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (= E190) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ S193) 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.
A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
38% identity, 61% coverage: 3:169/276 of query aligns to 86:238/324 of A0R3C4
- A222 (= A153) 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, 89% coverage: 3:249/276 of query aligns to 86:282/325 of P96379
- A219 (= A153) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
37% identity, 34% coverage: 3:95/276 of query aligns to 86:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
25% identity, 29% coverage: 21:100/276 of query aligns to 16:95/114 of 2yxhA
Query Sequence
>WP_013983285.1 NCBI__GCF_000013785.1:WP_013983285.1
MYQLPDLLHLMARLRDPQHGCPWDLQQDYASIVPHTLEEAYEVADAIESGDFEHLPGELG
DLLFQVVYYSQLAREEGRFDFATVVDAITRKLVRRHPHVFPDGDLYGSPELPRLDEAAIK
RRWEEIKAEERAEKAAAPEQLSLLDDVPSALPALSRAAKLQKRAAQVGFDWPEALPVVDK
VREELDEVLEAMSENDPQAIAEELGDLLFVVVNLARHLKVDPENALRAANGKFERRFRFI
EQALRDAGRPIENCDLEELDALWGEAKKAERSPSCG
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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