Comparing WP_068173905.1 NCBI__GCF_001592305.1:WP_068173905.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 8 hits to proteins with known functional sites (download)
3fijA Crystal structure of a uncharacterized protein lin1909
37% identity, 66% coverage: 65:250/280 of query aligns to 37:224/224 of 3fijA
O33341 Putative glutamine amidotransferase Rv2859c; EC 2.4.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 64% coverage: 66:245/280 of query aligns to 120:294/308 of O33341
7d50B Spua mutant - h221n with glutamyl-thioester (see paper)
38% identity, 60% coverage: 66:233/280 of query aligns to 60:231/255 of 7d50B
7d53A Spua mutant - h221n with glu (see paper)
38% identity, 60% coverage: 66:233/280 of query aligns to 54:225/249 of 7d53A
7d4rB Spua native structure (see paper)
41% identity, 45% coverage: 108:233/280 of query aligns to 65:193/215 of 7d4rB
6vtvB Crystal structure of puud gamma-glutamyl-gamma-aminobutyrate hydrolase from e. Coli
30% identity, 61% coverage: 63:232/280 of query aligns to 53:224/252 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)
30% identity, 61% coverage: 63:232/280 of query aligns to 55:226/254 of P76038
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
31% identity, 43% coverage: 116:234/280 of query aligns to 97:196/693 of P49915
Sites not aligning to the query:
>WP_068173905.1 NCBI__GCF_001592305.1:WP_068173905.1
MTLRIGISARLLHDPPPGLGLPQKRLQFLESSMAHWIMAHRAIALMVPFIDEESPLSANR
APMTELVDLLDGLVLQGGIDICPETYGDTLRDPAWAGDAVRDRYELNLLRGFIAAGKPVL
GVCRGAQLINVYFGGSLVQDIPSQRPGTIQHQDTTRYDRLTHEVHFETGSSLQRLYGNSV
PHRVTSIHHQCVDRLGEGLVVEAVSSKDGIIEAIRHTGPGYVLGVQWHPEFHLTPGEEMQ
GLLDSGPMMMDFLRAALARADRHQSGAAVVHPGVPLSARS
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