Comparing WP_086508348.1 NCBI__GCF_002151265.1:WP_086508348.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P02915 Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP; EC 7.4.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
64% identity, 96% coverage: 8:252/256 of query aligns to 7:253/258 of P02915
1b0uA Atp-binding subunit of the histidine permease from salmonella typhimurium (see paper)
64% identity, 96% coverage: 8:252/256 of query aligns to 3:249/258 of 1b0uA
3c4jA Abc protein artp in complex with atp-gamma-s
51% identity, 97% coverage: 8:256/256 of query aligns to 4:242/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
51% identity, 97% coverage: 8:256/256 of query aligns to 4:242/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
51% identity, 97% coverage: 8:256/256 of query aligns to 4:242/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
51% identity, 97% coverage: 8:256/256 of query aligns to 4:242/242 of 2oljA
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
52% identity, 95% coverage: 10:253/256 of query aligns to 4:237/240 of 4ymuJ
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
51% identity, 96% coverage: 8:252/256 of query aligns to 3:236/241 of 4u00A
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 96% coverage: 8:252/256 of query aligns to 2:241/343 of P30750
Sites not aligning to the query:
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
36% identity, 96% coverage: 8:252/256 of query aligns to 3:242/344 of 6cvlD
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
36% identity, 96% coverage: 8:252/256 of query aligns to 3:242/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
36% identity, 96% coverage: 8:252/256 of query aligns to 3:242/344 of 3tuiC
2pclA Crystal structure of abc transporter with complex (aq_297) from aquifex aeolicus vf5
43% identity, 81% coverage: 8:215/256 of query aligns to 4:202/223 of 2pclA
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
35% identity, 94% coverage: 13:252/256 of query aligns to 32:263/382 of 7ahhC
Sites not aligning to the query:
7aheC Opua inhibited inward facing (see paper)
35% identity, 94% coverage: 13:252/256 of query aligns to 32:263/382 of 7aheC
Sites not aligning to the query:
7ahdC Opua (e190q) occluded (see paper)
35% identity, 93% coverage: 13:249/256 of query aligns to 32:260/260 of 7ahdC
Sites not aligning to the query:
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
39% identity, 81% coverage: 4:211/256 of query aligns to 2:203/648 of P75831
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
36% identity, 84% coverage: 8:223/256 of query aligns to 4:214/226 of 5xu1B
2d62A Crystal structure of multiple sugar binding transport atp-binding protein
33% identity, 95% coverage: 12:253/256 of query aligns to 11:244/375 of 2d62A
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
37% identity, 80% coverage: 8:211/256 of query aligns to 4:202/592 of 5lj7A
>WP_086508348.1 NCBI__GCF_002151265.1:WP_086508348.1
MADTPIPLEVRNIKKRFGDTEVLKGLSLEARKGDVITLIGASGSGKSTFLRCMNLLEQPD
EGDLIVHGEEIRFKHTKHGREPADWKQVVRMRAKLSMVFQSFNLWSHMTLLENVIEAPIH
VLGKPKKEAIEHARALLDRVGLTARADAYPAQMSGGQQQRGAIARALAMDPEVMLFDEPT
SALDPELVGDVLKVMRDLAEEGRTMVVVTHEMGFARDVSSQVIYLHQGLVEEAGPPQEVL
VNPTSPRLKQFLAPKY
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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