Comparing WP_051453445.1 NCBI__GCF_000526715.1:WP_051453445.1 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)
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
54% identity, 92% coverage: 15:239/244 of query aligns to 3:226/226 of 5xu1B
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
50% identity, 91% coverage: 15:237/244 of query aligns to 1:227/232 of 1f3oA
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
50% identity, 91% coverage: 15:237/244 of query aligns to 1:227/230 of 1l2tA
5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
46% identity, 91% coverage: 15:236/244 of query aligns to 3:223/615 of 5lilA
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
46% identity, 91% coverage: 15:236/244 of query aligns to 3:223/592 of 5lj7A
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
45% identity, 95% coverage: 13:243/244 of query aligns to 2:231/648 of P75831
5ws4A Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
47% identity, 91% coverage: 15:237/244 of query aligns to 4:225/650 of 5ws4A
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
44% identity, 89% coverage: 15:231/244 of query aligns to 5:221/233 of P75957
7arlD Lolcde in complex with lipoprotein and adp (see paper)
44% identity, 89% coverage: 15:231/244 of query aligns to 2:218/222 of 7arlD
7mdyC Lolcde nucleotide-bound
44% identity, 89% coverage: 15:231/244 of query aligns to 2:218/226 of 7mdyC
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
44% identity, 89% coverage: 15:231/244 of query aligns to 4:220/229 of 7v8iD
2pclA Crystal structure of abc transporter with complex (aq_297) from aquifex aeolicus vf5
44% identity, 83% coverage: 31:233/244 of query aligns to 15:216/223 of 2pclA
8g4cB Bceabs atpgs high res tm (see paper)
38% identity, 87% coverage: 21:233/244 of query aligns to 9:221/248 of 8g4cB
7tchB Bceab e169q variant atp-bound conformation (see paper)
38% identity, 87% coverage: 21:233/244 of query aligns to 8:220/245 of 7tchB
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 91% coverage: 15:236/244 of query aligns to 1:223/343 of P30750
Sites not aligning to the query:
8iddA Cryo-em structure of mycobacterium tuberculosis atp bound ftsex/ripc complex in peptidisc (see paper)
43% identity, 91% coverage: 15:236/244 of query aligns to 2:220/225 of 8iddA
A5U7B7 Cell division ATP-binding protein FtsE from Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) (see 2 papers)
43% identity, 91% coverage: 15:236/244 of query aligns to 1:219/229 of A5U7B7
8igqA Cryo-em structure of mycobacterium tuberculosis adp bound ftsex/ripc complex in peptidisc (see paper)
43% identity, 91% coverage: 15:236/244 of query aligns to 2:220/227 of 8igqA
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
37% identity, 91% coverage: 15:236/244 of query aligns to 2:224/344 of 6cvlD
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
37% identity, 91% coverage: 15:236/244 of query aligns to 2:224/344 of 3tuzC
Sites not aligning to the query:
>WP_051453445.1 NCBI__GCF_000526715.1:WP_051453445.1
MWSSDNNNNTRETPLIAFKDITKTYGQGASAFTALKGVNFQIESGEFVAIMGPSGSGKST
VMNTLGCLDIPSSGHYYFQGVAVESLTHDQRALLRRHYLGFVFQGFNLLARTSAIENVEL
PLLYRGMKTAERRAEARKALALVGLGGWENHAPSELSGGQQQRVAIARALVTHPKVLLAD
EPTGNLDTQRSREIMELLSQLNKELGITVIMVTHESEMADYAHRLIHFIDGMVEKDHTQA
ERTV
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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