Comparing PfGW456L13_602 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_602 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)
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
48% identity, 100% coverage: 1:334/335 of query aligns to 1:340/343 of P30750
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
48% identity, 100% coverage: 1:334/335 of query aligns to 2:341/344 of 3tuzC
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
48% identity, 100% coverage: 1:334/335 of query aligns to 2:341/344 of 3tuiC
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
48% identity, 100% coverage: 1:334/335 of query aligns to 2:341/344 of 6cvlD
4u00A Crystal structure of ttha1159 in complex with adp (see paper)
45% identity, 73% coverage: 1:243/335 of query aligns to 2:237/241 of 4u00A
4ymuJ Crystal structure of an amino acid abc transporter complex with arginines and atps (see paper)
42% identity, 71% coverage: 7:244/335 of query aligns to 4:238/240 of 4ymuJ
3c4jA Abc protein artp in complex with atp-gamma-s
43% identity, 71% coverage: 6:244/335 of query aligns to 5:240/242 of 3c4jA
3c41J Abc protein artp in complex with amp-pnp/mg2+
43% identity, 71% coverage: 6:244/335 of query aligns to 5:240/242 of 3c41J
2olkA Abc protein artp in complex with adp-beta-s
43% identity, 71% coverage: 6:244/335 of query aligns to 5:240/242 of 2olkA
2oljA Abc protein artp in complex with adp/mg2+
43% identity, 71% coverage: 6:244/335 of query aligns to 5:240/242 of 2oljA
P0A9R7 Cell division ATP-binding protein FtsE from Escherichia coli (strain K12) (see paper)
44% identity, 65% coverage: 1:218/335 of query aligns to 1:213/222 of P0A9R7
8w6iD Cryo-em structure of escherichia coli str k12 ftsex complex with atp- gamma-s in peptidisc
45% identity, 62% coverage: 1:207/335 of query aligns to 1:202/219 of 8w6iD
8hd0A Cell divisome spg hydrolysis machinery ftsex-envc
43% identity, 65% coverage: 1:218/335 of query aligns to 1:213/218 of 8hd0A
8tzjA Cryo-em structure of vibrio cholerae ftse/ftsx complex (see paper)
43% identity, 61% coverage: 1:205/335 of query aligns to 2:201/220 of 8tzjA
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)
42% identity, 71% coverage: 6:243/335 of query aligns to 11:254/258 of P02915
7ahhC Opua inhibited inward-facing, sbd docked (see paper)
37% identity, 67% coverage: 20:244/335 of query aligns to 41:265/382 of 7ahhC
Sites not aligning to the query:
7aheC Opua inhibited inward facing (see paper)
37% identity, 67% coverage: 20:244/335 of query aligns to 41:265/382 of 7aheC
Sites not aligning to the query:
1b0uA Atp-binding subunit of the histidine permease from salmonella typhimurium (see paper)
42% identity, 71% coverage: 6:243/335 of query aligns to 7:250/258 of 1b0uA
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
39% identity, 66% coverage: 1:220/335 of query aligns to 3:220/226 of 5xu1B
5d3mA Folate ecf transporter: amppnp bound state (see paper)
40% identity, 72% coverage: 1:241/335 of query aligns to 5:240/280 of 5d3mA
>PfGW456L13_602 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_602
VIEFQNVHKTYRVAGKEIPALHPTSLTIENGQVYGLIGHSGAGKSTLLRLINRLENASGG
KITVDGEEVTALDANGLRRFRQQVGMIFQHFNLLASKTVADNVALPLTLAGELSRSEIDS
RVAELLARVGLSDHAKKYPAQLSGGQKQRVGIARALATKPKILLCDEATSALDPQTTASV
LQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDAGVIVEQGSVAEVFLHPKHPTTKR
FVQEDEQIDESEQRDDFAHVPGRIVRLTFQGDATYAPLLGTVARETGVDYSILAGRIDRI
KDIPYGQLTLAVTGGDMEAAFARFTAADVHMEVLR
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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