Comparing 349787 FitnessBrowser__Btheta:349787 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 16 hits to proteins with known functional sites (download)
Q9UYV8 Nitrilase; PaNit; EC 3.5.5.1 from Pyrococcus abyssi (strain GE5 / Orsay) (see paper)
30% identity, 84% coverage: 36:255/261 of query aligns to 35:257/262 of Q9UYV8
3klcB Crystal structure of hyperthermophilic nitrilase (see paper)
30% identity, 84% coverage: 36:255/261 of query aligns to 34:256/261 of 3klcB
Sites not aligning to the query:
3klcA Crystal structure of hyperthermophilic nitrilase (see paper)
30% identity, 84% coverage: 36:255/261 of query aligns to 34:256/261 of 3klcA
Sites not aligning to the query:
Q9NQR4 Omega-amidase NIT2; Nitrilase homolog 2; EC 3.5.1.3 from Homo sapiens (Human) (see 2 papers)
26% identity, 96% coverage: 1:251/261 of query aligns to 1:262/276 of Q9NQR4
6ypaB The c146a variant of an amidase from pyrococcus horikoshii with bound glutaramide
29% identity, 84% coverage: 36:255/261 of query aligns to 42:264/269 of 6ypaB
7ovgA The c146a variant of an amidase from pyrococcus horikoshii with bound acetamide (see paper)
29% identity, 84% coverage: 36:255/261 of query aligns to 36:258/263 of 7ovgA
Q94JV5 Deaminated glutathione amidase, chloroplastic/cytosolic; dGSH amidase; Nitrilase-like protein 2; Protein nitrilase 1 homolog; AtNit1; Protein Nit1 homolog; EC 3.5.1.128 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 66% coverage: 79:251/261 of query aligns to 128:300/307 of Q94JV5
Sites not aligning to the query:
4iztA The e41q mutant of the amidase from nesterenkonia sp. An1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine
24% identity, 82% coverage: 4:218/261 of query aligns to 10:229/263 of 4iztA
4izuA The e41q mutant of the amidase from nesterenkonia sp. An1 showing the result of michael addition of acrylamide at the active site cysteine
24% identity, 82% coverage: 4:218/261 of query aligns to 2:221/254 of 4izuA
O25067 Aliphatic amidase; Acylamide amidohydrolase; EC 3.5.1.4 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
25% identity, 46% coverage: 125:245/261 of query aligns to 146:267/339 of O25067
P47016 Deaminated glutathione amidase; dGSH amidase; Nitrilase homolog 1; EC 3.5.1.128 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 62% coverage: 88:250/261 of query aligns to 105:298/307 of P47016
4hg5A Structural insights into yeast nit2: wild-type yeast nit2 in complex with oxaloacetate (see paper)
26% identity, 62% coverage: 88:250/261 of query aligns to 102:295/304 of 4hg5A
4hg3A Structural insights into yeast nit2: wild-type yeast nit2 in complex with alpha-ketoglutarate (see paper)
26% identity, 62% coverage: 88:250/261 of query aligns to 102:295/304 of 4hg3A
P11436 Aliphatic amidase; Acylamide amidohydrolase; EC 3.5.1.4 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
28% identity, 43% coverage: 134:244/261 of query aligns to 157:267/346 of P11436
Sites not aligning to the query:
Q9RQ17 Aliphatic amidase; Acylamide amidohydrolase; Wide spectrum amidase; EC 3.5.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
26% identity, 43% coverage: 134:245/261 of query aligns to 157:268/348 of Q9RQ17
Sites not aligning to the query:
4gylA The e142l mutant of the amidase from geobacillus pallidus showing the result of michael addition of acrylamide at the active site cysteine (see paper)
27% identity, 43% coverage: 134:245/261 of query aligns to 157:268/340 of 4gylA
Sites not aligning to the query:
>349787 FitnessBrowser__Btheta:349787
MDSIRISIVQTDIVWENKQENLRLLHEKLQSLCGTTEIVVLPEMFSTGFSMQSDMLAEAN
SGETITTLKQWASLFQVAICGSYITVDNGRYYNRAFFLTPEGEEFYYDKRHLFRMGREAE
HFSAGDERLIIPYRGWNICLLVCYDLRFPVWSRNVANQYDLLIYVANWPIPRRLAWDTLL
RARALENQCYVCGVNRVGIDGYRLKYNGGSKIYSALGEEAASVPDETEGIATATLHLTAL
HQFREKFPVWKDADEFQLRHS
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory