Comparing BPHYT_RS15045 FitnessBrowser__BFirm:BPHYT_RS15045 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
3fijA Crystal structure of a uncharacterized protein lin1909
42% identity, 34% coverage: 306:473/493 of query aligns to 42:208/224 of 3fijA
O33341 Putative glutamine amidotransferase Rv2859c; EC 2.4.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
39% identity, 32% coverage: 306:465/493 of query aligns to 124:279/308 of O33341
Sites not aligning to the query:
7d50B Spua mutant - h221n with glutamyl-thioester (see paper)
39% identity, 34% coverage: 306:475/493 of query aligns to 64:238/255 of 7d50B
7d53A Spua mutant - h221n with glu (see paper)
39% identity, 34% coverage: 306:475/493 of query aligns to 58:232/249 of 7d53A
P76038 Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD; Gamma-Glu-GABA hydrolase; EC 3.5.1.94 from Escherichia coli (strain K12) (see paper)
30% identity, 43% coverage: 257:467/493 of query aligns to 19:226/254 of P76038
6vtvB Crystal structure of puud gamma-glutamyl-gamma-aminobutyrate hydrolase from e. Coli
30% identity, 43% coverage: 257:467/493 of query aligns to 17:224/252 of 6vtvB
7d4rB Spua native structure (see paper)
41% identity, 27% coverage: 344:475/493 of query aligns to 65:200/215 of 7d4rB
>BPHYT_RS15045 FitnessBrowser__BFirm:BPHYT_RS15045
MSENKPENAGKPGNPTPPSASPAPSGTTPGASIAGSVPPDPAASLPLSHEDAIQSPVKDV
TPPDVASTSTPAAEEAAVRSSTDDPDSASAVTPTDPQKARQRDAAEARSSAAASTARQEA
EVHERDARRAGVHAMRPSPTVGGSEPVDGELVGAVEDVTVNEEIPASAERRAGSPPPGFG
AAPDFTASNPPPPNALPPSPPPRYLKHSDSAWTVFGRIVAARARQIFDRAGQRITQRTLR
IGVSARIFHPEPGAKGLRGKTLQYLEESIAHWVMSRDVLVFMIPTVGHQGMLHPSNIRLR
DYAKHLDGLLLQGGADVSPQSYAEQAASHEWPGDRVRDMYELELLHEFVESGKPVLGVCR
GCQLINVAFGGTLYQDIATDVPTAATHVNENYDQHRHGIHFPDGSTLANMFPGRRDAIVN
SIHHQAVKTLGRDLNIEAVSASDGIIEAVRYRRAPFVMGVQWHPEFHRAGGPELLDCTPL
LDTFLRVARETRF
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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