SitesBLAST
Comparing 206069 MicrobesOnline__882:206069 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 hits to proteins with known functional sites (download)
P15029 Fe(3+) dicitrate transport system permease protein FecD; Iron(III) dicitrate transport system permease protein FecD from Escherichia coli (strain K12) (see paper)
38% identity, 82% coverage: 60:346/351 of query aligns to 46:318/318 of P15029
- R51 (= R65) mutation to C: Retains 32% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 14% of wild-type citrate-mediated Fe(3+) transport.
- R54 (= R68) mutation to C: Retains 19% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 24% of wild-type citrate-mediated Fe(3+) transport.
- R288 (= R315) mutation to C: Retains 65% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 35% of wild-type citrate-mediated Fe(3+) transport.
P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
34% identity, 84% coverage: 51:345/351 of query aligns to 46:331/332 of P15030
- R60 (= R65) mutation to C: Retains 33% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 29% of wild-type citrate-mediated Fe(3+) transport.
- R63 (= R68) mutation to C: Retains 74% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 30% of wild-type citrate-mediated Fe(3+) transport.
- R302 (= R315) mutation to C: Retains 24% of wild-type citrate-mediated Fe(3+) transport.; mutation to E: Retains 28% of wild-type citrate-mediated Fe(3+) transport.
5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
38% identity, 81% coverage: 63:346/351 of query aligns to 56:328/330 of 5b57A
P06972 Iron(3+)-hydroxamate import system permease protein FhuB; Ferric hydroxamate uptake protein B; Ferrichrome transport system permease protein FhuB; Ferrichrome uptake protein FhuB; Iron(III)-hydroxamate import system permease protein FhuB from Escherichia coli (strain K12) (see paper)
34% identity, 81% coverage: 50:334/351 of query aligns to 43:315/660 of P06972
- S57 (≠ I64) mutation to A: Decreased binding to ferrichrome-FhuD.
- D170 (≠ E189) mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-171.
- Q171 (≠ S190) mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-170.
- M175 (≠ I194) mutation to A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-484; A-492 and A-495.; mutation to L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-484; L-492 and L-495.
- T182 (≠ S201) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-184.
- T184 (≠ Q203) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-182.
- E304 (= E323) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
Sites not aligning to the query:
- 390 Interaction with FhuD; R→A: Decreased binding to ferrichrome-FhuD.
- 484 M→A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-492 and A-495.; M→L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-492 and L-495.
- 492 M→A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-495.; M→L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-495.
- 495 M→A: No effect on ATPase activity, but 80% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with A-175; A-484 and A-492.; M→L: No effect on ATPase activity, but 50% decrease in Fe-ferrichrome transport efficiency of the FhuCB complex compared to wild-type; when associated with L-175; L-484 and L-492.
- 507 Q→A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
- 510 T→A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
- 515 Interaction with FhuD; S→A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
- 517 Interaction with FhuD; Y→A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
- 636 Q→A: Decreased binding to ferrichrome-FhuD.
Query Sequence
>206069 MicrobesOnline__882:206069
MSRIRRRTALALGAALWLLSVPAACLFGPFDIGPAEVMRLLGAAAGVPVSGHVDPIRLLV
VGDIRLARVCLSLLVGGGLAMAGVVFQGVLRNPLADPFTLGVSSGAALGASVAISFGVTL
PAAVAPALVAGLGVVTPAALFGAFAALSLVLLLGTAAGSFRRETVVLAGVVVSTFLAALV
SLVKALDEESVSSIVFWIMGSLQGRGWAHTAVLLPPLVLGLAAVVRHARDLDVLALGDTQ
ASQLGMRTGYVRCVLLCGASCITAGCVAVSGVIGFVGLVVPHLLRLVLGAAHGPLLIGAW
FGGGILLLWSDVVARTLLSGGAELPVGVVTALVGGPFFCLLLQREQRRERP
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory