Comparing SMc04383 FitnessBrowser__Smeli:SMc04383 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)
Q88CC1 2-oxoadipate dioxygenase/decarboxylase; 2-hydroxyglutarate synthase; EC 1.13.11.93 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
60% identity, 99% coverage: 1:460/466 of query aligns to 1:460/464 of Q88CC1
6w1hA Crystal structure of the hydroxyglutarate synthase in complex with 2- oxoadipate from pseudomonas putida (see paper)
59% identity, 98% coverage: 4:460/466 of query aligns to 2:449/450 of 6w1hA
2rjbA Crystal structure of uncharacterized protein ydcj (sf1787) from shigella flexneri which includes domain duf1338. Northeast structural genomics consortium target sfr276
53% identity, 96% coverage: 7:455/466 of query aligns to 4:416/418 of 2rjbA
2rjbC Crystal structure of uncharacterized protein ydcj (sf1787) from shigella flexneri which includes domain duf1338. Northeast structural genomics consortium target sfr276
49% identity, 96% coverage: 7:455/466 of query aligns to 1:362/364 of 2rjbC
2rjbD Crystal structure of uncharacterized protein ydcj (sf1787) from shigella flexneri which includes domain duf1338. Northeast structural genomics consortium target sfr276
53% identity, 89% coverage: 7:421/466 of query aligns to 1:365/372 of 2rjbD
>SMc04383 FitnessBrowser__Smeli:SMc04383
MKENSFVSADDIRSAFSAAMSLMYREEVPAYGTLMELVARVNGETLSADATLKGRLEATD
SLERISEERHGAIRLGTPAELSMMRRVFAVMGMYPVGYYDLSTAGVPVHSTAFRPVGDAA
LKHNPFRVFTSLLRLDLISDEALRAEAEAILKERRIFTSGAVELTEKAERDGGLDKADAE
RFVAEVLETFRWHDEANVSAGMYERLHDAHRLIADVVSFKGPHINHLTPRTLDIDRVQAL
MPEYGIAPKAVVEGPPTRKCPVLLRQTSFKALEEPVSFRDSDGSWKTGSHTARFGEIEQR
GIALTPKGRGLYDRLLDESRKIVRPAADGSNAREYEAALAQVFEAFPDSWAELREAGLGY
FSYSLTDKGRRTKLPGRRDLNSLIADGLVQFDPIVYEDFLPVSAAGIFQSNLGDGAQQEF
EASPNQKRFETDLGVAVLNEFDHYAGIEQASIEGCLKALTAAMAAE
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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