Comparing Dsui_2877 Dsui_2877 ABC-type antimicrobial peptide transport system, ATPase component 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)
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
52% identity, 90% coverage: 13:234/248 of query aligns to 3:224/226 of 5xu1B
5ws4A Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
50% identity, 92% coverage: 12:239/248 of query aligns to 3:230/650 of 5ws4A
5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
49% identity, 90% coverage: 13:234/248 of query aligns to 3:224/615 of 5lilA
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
49% identity, 90% coverage: 13:234/248 of query aligns to 3:224/592 of 5lj7A
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
48% identity, 90% coverage: 13:235/248 of query aligns to 4:226/648 of P75831
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
48% identity, 88% coverage: 13:230/248 of query aligns to 1:223/232 of 1f3oA
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
48% identity, 88% coverage: 13:230/248 of query aligns to 1:223/230 of 1l2tA
2pclA Crystal structure of abc transporter with complex (aq_297) from aquifex aeolicus vf5
47% identity, 82% coverage: 30:233/248 of query aligns to 16:219/223 of 2pclA
7mdyC Lolcde nucleotide-bound
45% identity, 88% coverage: 13:231/248 of query aligns to 2:221/226 of 7mdyC
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
45% identity, 88% coverage: 13:231/248 of query aligns to 5:224/233 of P75957
7arlD Lolcde in complex with lipoprotein and adp (see paper)
45% identity, 88% coverage: 13:231/248 of query aligns to 2:221/222 of 7arlD
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
44% identity, 88% coverage: 13:231/248 of query aligns to 4:223/229 of 7v8iD
8g4cB Bceabs atpgs high res tm (see paper)
36% identity, 88% coverage: 12:230/248 of query aligns to 2:221/248 of 8g4cB
6z4wA Ftse structure from streptococcus pneumoniae in complex with adp (space group p 1) (see paper)
40% identity, 90% coverage: 12:233/248 of query aligns to 2:220/230 of 6z4wA
7tchB Bceab e169q variant atp-bound conformation (see paper)
36% identity, 88% coverage: 12:230/248 of query aligns to 1:220/245 of 7tchB
6z67B Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a resolution (see paper)
40% identity, 90% coverage: 11:233/248 of query aligns to 1:220/229 of 6z67B
8iddA Cryo-em structure of mycobacterium tuberculosis atp bound ftsex/ripc complex in peptidisc (see paper)
46% identity, 82% coverage: 31:233/248 of query aligns to 18:220/225 of 8iddA
Sites not aligning to the query:
8igqA Cryo-em structure of mycobacterium tuberculosis adp bound ftsex/ripc complex in peptidisc (see paper)
46% identity, 82% coverage: 31:233/248 of query aligns to 18:220/227 of 8igqA
Sites not aligning to the query:
A5U7B7 Cell division ATP-binding protein FtsE from Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) (see 2 papers)
46% identity, 82% coverage: 31:233/248 of query aligns to 17:219/229 of A5U7B7
P0A9R7 Cell division ATP-binding protein FtsE from Escherichia coli (strain K12) (see paper)
41% identity, 88% coverage: 13:230/248 of query aligns to 1:215/222 of P0A9R7
>Dsui_2877 Dsui_2877 ABC-type antimicrobial peptide transport system, ATPase component
MSAATASADAAAVIEVAGLDKAYDTPMGPFPVLKGVSLAIHAGEFVAIMGPSGSGKSTFM
NILGCLDRPSGGDYILDGKHVSALDKDQTALLRNRTIGFVFQGFNLLPRMSLEDNVALPL
VYCGVDKEERRQRARELLAKVGLGQYAKSLPNRISGGQQQRVAIARALVNRPRLILADEP
TGNLDSHTSEEIMALFEELNREGITIVLVTHEPDIAQHAKRQVRFLDGRIVHDAPTHHDL
PAGEAQPC
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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