Comparing Pf1N1B4_4353 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4353 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)
73% identity, 99% coverage: 1:250/253 of query aligns to 6:255/255 of 7d50B
7d53A Spua mutant - h221n with glu (see paper)
74% identity, 97% coverage: 5:250/253 of query aligns to 4:249/249 of 7d53A
7d4rB Spua native structure (see paper)
64% identity, 96% coverage: 5:248/253 of query aligns to 2:215/215 of 7d4rB
P76038 Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD; Gamma-Glu-GABA hydrolase; EC 3.5.1.94 from Escherichia coli (strain K12) (see paper)
44% identity, 97% coverage: 4:248/253 of query aligns to 7:249/254 of P76038
6vtvB Crystal structure of puud gamma-glutamyl-gamma-aminobutyrate hydrolase from e. Coli
44% identity, 97% coverage: 4:248/253 of query aligns to 5:247/252 of 6vtvB
3fijA Crystal structure of a uncharacterized protein lin1909
31% identity, 96% coverage: 3:245/253 of query aligns to 1:222/224 of 3fijA
O33341 Putative glutamine amidotransferase Rv2859c; EC 2.4.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
33% identity, 96% coverage: 2:243/253 of query aligns to 63:295/308 of O33341
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
28% identity, 51% coverage: 101:229/253 of query aligns to 92:198/693 of P49915
Sites not aligning to the query:
>Pf1N1B4_4353 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4353
MAFKPLIGVTACIKQIGLHPYHVSGDKYLRAVSVAALGLPVVIPSLGELTEIDDLLAQLD
GLLLTGSPSNVEPFHYQGPASAPGTDHDPQRDATTLPLLRAAIAAGVPVLGICRGFQEMN
VAFGGSLHQKVHELPGMLDHREADHPDLAVQYAPAHAVSVQPGGVFEALDLPQVFQVNSI
HSQGIDRLAPGLRAEAVAPDGLIEAISVEHSKAFAVGVQWHPEWQVLSNPPYLSIFQAFG
DACRQRAALRNTR
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