SitesBLAST
Comparing BWI76_RS22800 FitnessBrowser__Koxy:BWI76_RS22800 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)
89% identity, 100% coverage: 1:263/263 of query aligns to 1:263/263 of P0AEY3
- R95 (= R95) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K119 (= K119) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
- K168 (= K168) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KVYEE 168:172 (≠ KVHEE 168:172) binding
- E171 (= E171) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E172 (= E172) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- E175 (= E175) binding ; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- K189 (= K189) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- KLEE 189:192 (= KLEE 189:192) binding
- E192 (= E192) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
- E193 (= E193) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- D196 (= D196) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K222 (= K222) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- KFERR 222:226 (= KFERR 222:226) binding
- R226 (= R226) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- W253 (= W253) binding ; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
- K257 (= K257) 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)
78% identity, 98% coverage: 2:260/263 of query aligns to 1:225/225 of 3crcA
3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
76% identity, 98% coverage: 2:260/263 of query aligns to 1:219/220 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)
41% identity, 97% coverage: 4:257/263 of query aligns to 8:250/255 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 (= K119) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
- E173 (≠ A180) mutation to A: Has little effects on the NTPase activity.
- E176 (≠ A183) mutation to A: Has little effects on the NTPase activity.
- EE 185:186 (= EE 192:193) 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, 57% coverage: 8:157/263 of query aligns to 91:238/324 of A0R3C4
- A222 (= A141) 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)
38% identity, 57% coverage: 8:157/263 of query aligns to 91:235/325 of P96379
- A219 (= A141) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.
7yh5B Mazg(mycobacterium tuberculosis) (see paper)
41% identity, 33% coverage: 8:95/263 of query aligns to 91:177/177 of 7yh5B
2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 47% coverage: 4:126/263 of query aligns to 2:107/114 of 2yxhA
Query Sequence
>BWI76_RS22800 FitnessBrowser__Koxy:BWI76_RS22800
MSQIDRLLGIMQRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAIAREDFDDLRGELG
DLLFQVVFYAQMAQEEGRFDFNDICAAIGDKLERRHPHIFGDASAGNSSEVLARWEQIKS
AERAEKSQHSALDDIPHSLPALMRAHKIQKRCSAVGFDWTSLGPVLDKVHEEIDEVMHEA
QQAVVDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANLKFERRFREVERIVAARGLE
MTGVDLDTMELVWQEVKRQETDL
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