Comparing CCNA_03234 FitnessBrowser__Caulo:CCNA_03234 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 8 hits to proteins with known functional sites (download)
7d50B Spua mutant - h221n with glutamyl-thioester (see paper)
40% identity, 97% coverage: 1:241/249 of query aligns to 6:247/255 of 7d50B
7d53A Spua mutant - h221n with glu (see paper)
40% identity, 96% coverage: 4:241/249 of query aligns to 4:241/249 of 7d53A
7d4rB Spua native structure (see paper)
36% identity, 96% coverage: 4:241/249 of query aligns to 2:209/215 of 7d4rB
6vtvB Crystal structure of puud gamma-glutamyl-gamma-aminobutyrate hydrolase from e. Coli
36% identity, 96% coverage: 1:238/249 of query aligns to 3:238/252 of 6vtvB
P76038 Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD; Gamma-Glu-GABA hydrolase; EC 3.5.1.94 from Escherichia coli (strain K12) (see paper)
36% identity, 96% coverage: 1:238/249 of query aligns to 5:240/254 of P76038
3fijA Crystal structure of a uncharacterized protein lin1909
32% identity, 86% coverage: 25:238/249 of query aligns to 11:216/224 of 3fijA
O33341 Putative glutamine amidotransferase Rv2859c; EC 2.4.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 89% coverage: 2:222/249 of query aligns to 64:279/308 of O33341
Sites not aligning to the query:
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
31% identity, 52% coverage: 100:228/249 of query aligns to 92:198/693 of P49915
Sites not aligning to the query:
>CCNA_03234 FitnessBrowser__Caulo:CCNA_03234
MTRPVAGIICCTRTVGVEPAQAVMSRYVDATMAYGDVAALLIPSLPGRMRAAEVAGRLDG
LMLTGSPSNLDPALYGEEIGDAPGPFDAARDGMTADLIKAMLDLGKPVFGICRGFQEINV
AFGGTLRRDTSSSSDLIDHHAPEDVSFEAMFDHVHAVKLMRGGVLERAFGVQAAVVNSVH
YQGVDRLGEGLSVEALSEDDLVEAFSATVNGAPVLAVQWHPEWKPAQNRQSQIFFEVFGR
ALRGAPLVA
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