Comparing 200832 FitnessBrowser__MR1:200832 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 5 hits to proteins with known functional sites (download)
Q02I31 Putative pterin-4-alpha-carbinolamine dehydratase; PHS; 4-alpha-hydroxy-tetrahydropterin dehydratase; Pterin carbinolamine dehydratase; PCD; EC 4.2.1.96 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
76% identity, 96% coverage: 1:108/112 of query aligns to 1:108/118 of Q02I31
2v6tB Crystal structure of a complex of pterin-4a-carbinolamine dehydratase from toxoplasma gondii with 7,8-dihydrobiopterin (see paper)
29% identity, 77% coverage: 23:108/112 of query aligns to 10:93/100 of 2v6tB
1f93A Crystal structure of a complex between the dimerization domain of hnf-1 alpha and the coactivator dcoh (see paper)
28% identity, 80% coverage: 16:105/112 of query aligns to 4:93/103 of 1f93A
P61459 Pterin-4-alpha-carbinolamine dehydratase; PHS; 4-alpha-hydroxy-tetrahydropterin dehydratase; Dimerization cofactor of hepatocyte nuclear factor 1-alpha; DCoH; Dimerization cofactor of HNF1; Phenylalanine hydroxylase-stimulating protein; Pterin carbinolamine dehydratase; PCD; EC 4.2.1.96 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 80% coverage: 16:105/112 of query aligns to 5:94/104 of P61459
Sites not aligning to the query:
P61457 Pterin-4-alpha-carbinolamine dehydratase; PHS; 4-alpha-hydroxy-tetrahydropterin dehydratase; Dimerization cofactor of hepatocyte nuclear factor 1-alpha; DCoH; Dimerization cofactor of HNF1; Phenylalanine hydroxylase-stimulating protein; Pterin carbinolamine dehydratase; PCD; EC 4.2.1.96 from Homo sapiens (Human) (see 6 papers)
28% identity, 80% coverage: 16:105/112 of query aligns to 5:94/104 of P61457
Sites not aligning to the query:
>200832 FitnessBrowser__MR1:200832
MTALTQMKCEACQADAPKVTDEELAELIRMIPDWGVQVRDGIMQLERVYKFKNFKLAMAF
TNKLAELAEEEFHHPGILTEWGKVTVTWWSHSIKGLHKNDFIMAAKTDLLLD
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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