Comparing BWI76_RS12435 FitnessBrowser__Koxy:BWI76_RS12435 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
O04373 IAA-amino acid hydrolase ILR1-like 4; jasmonoyl-L-amino acid hydrolase; EC 3.5.1.-; EC 3.5.1.127 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 96% coverage: 17:388/389 of query aligns to 49:423/440 of O04373
P54968 IAA-amino acid hydrolase ILR1; EC 3.5.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 95% coverage: 19:388/389 of query aligns to 55:427/442 of P54968
P54955 N-acetylcysteine deacetylase; S-(2-succino)cysteine metabolism operon protein P; EC 3.5.1.- from Bacillus subtilis (strain 168)
34% identity, 95% coverage: 15:383/389 of query aligns to 9:371/380 of P54955
4ewtA The crystal structure of a putative aminohydrolase from methicillin resistant staphylococcus aureus (see paper)
31% identity, 100% coverage: 1:389/389 of query aligns to 1:389/389 of 4ewtA
6slfA Nalpha-acylglutamine aminoacylase from corynebacterium sp.Releasing human axilla odorants co-crystallised with high affinity inhibitor (see paper)
35% identity, 86% coverage: 5:338/389 of query aligns to 8:344/398 of 6slfA
Sites not aligning to the query:
3ramA Crystal structure of hmra (see paper)
24% identity, 70% coverage: 5:278/389 of query aligns to 7:261/391 of 3ramA
Sites not aligning to the query:
>BWI76_RS12435 FitnessBrowser__Koxy:BWI76_RS12435
MTHPIIEALQVNEAQFVALRRRFHQQPEIGFEEHKTSEEVARLLGEWGYQVHRGLAGTGV
VATLSAGDGKKRLGLRADMDALPMQEMSGKAWASRVDGRFHGCGHDGHTTTLLYAAEYLA
RTRQFNGTLQLIFQPAEELLYGGRVMLEDGLFEQFPCDAIFGLHNMPGQPLGRVGLRDGA
MMASSDTLHIEVKGVGGHGAVPEHTVDATLVACHITLALQSIVSRNITPFEPAVVTVGSI
QAGHAPNIINDKVLMKLTVRTLNEQVRETVLQRIHDIAVAQAESFNASAALTHVNGSPVL
RNDPVANEMVRTVATALFGEAQVGEVKPFMGSEDFAFMLERNPNGCYFTLGAGDEADRCM
VHNPGYDFNDALLLKGAALWCALTEHYLR
Or try a new SitesBLAST search
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