SitesBLAST
Comparing AZOBR_RS17950 FitnessBrowser__azobra:AZOBR_RS17950 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 4 hits to proteins with known functional sites (download)
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)
44% identity, 94% coverage: 37:656/658 of query aligns to 44:660/660 of P06972
- S57 (= S50) mutation to A: Decreased binding to ferrichrome-FhuD.
- D170 (≠ E164) mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-171.
- Q171 (≠ Y165) mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-170.
- M175 (≠ I169) 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 (≠ A176) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-184.
- T184 (≠ A178) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-182.
- E304 (= E298) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
- R390 (= R385) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
- M484 (≠ I479) 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-175; 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-175; L-492 and L-495.
- M492 (≠ A487) 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-175; A-484 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-175; L-484 and L-495.
- M495 (≠ T490) 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-175; A-484 and A-492.; 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-175; L-484 and L-492.
- Q507 (≠ A502) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
- T510 (≠ R505) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
- S515 (= S510) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
- Y517 (≠ N512) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
- Q636 (= Q631) mutation to A: Decreased binding to ferrichrome-FhuD.
P15030 Fe(3+) dicitrate transport system permease protein FecC; Iron(III) dicitrate transport system permease protein FecC from Escherichia coli (strain K12) (see paper)
38% identity, 41% coverage: 385:652/658 of query aligns to 60:330/332 of P15030
- R60 (= R385) 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 (= R388) 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 (= R624) 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.
P15029 Fe(3+) dicitrate transport system permease protein FecD; Iron(III) dicitrate transport system permease protein FecD from Escherichia coli (strain K12) (see paper)
39% identity, 41% coverage: 380:652/658 of query aligns to 46:316/318 of P15029
- R51 (= R385) 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 (= R388) 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 (= R624) 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.
5b57A Inward-facing conformation of abc heme importer bhuuv from burkholderia cenocepacia (see paper)
34% identity, 41% coverage: 53:322/658 of query aligns to 60:328/330 of 5b57A
Sites not aligning to the query:
Query Sequence
>AZOBR_RS17950 FitnessBrowser__azobra:AZOBR_RS17950
MAVNRILLWSGLALAAAALSAWQVAGHAAAPSMPLPPDAAWLDGVILYHSVLPRIAVALV
AGAALGLSGLLLQRVLRNPLAEPSTLGVSAGAQLALTLGMLYAPALMDHAREGVALAGGL
AAVGLILAMTWRRGLEPVAVVLAGMMVALTATMGSAALILANGEYLFSIFLWGGGALAQQ
SWGPTLTIAVRLLIGVGAAVLLMRPLAILGLDDASARSLGVALNATRFGVIGVAVWLAAS
VTAEVGVIGFVGLAAPALAHLSGARTQGQRLVAAPLIGALLLWLTDGLVQLLAGVDGERV
PTGAATALLGGPLLLWLLPRLRMFEWPSLNSRPAPSRRSLHPYRLIALFAVLGAVAVGLA
LTVGYGPGGWTLSTGPLLDTLLGWRGPRVAVAAAAGAMLAAAGMLLQRVTANPLASPEIL
GVGTGAGVGLTAALFLVAAPGFGVQLAASAAGAVLTLAAMLALSLRAGFGPERLLLAGIA
MSALCSAVLTAVIATGTPQAFALLRWLSGSTNEAGPGDAWFCIGVAVLLLATLPLTAKWL
EILPLGDVTAQAVGLPVRRCRVLLVLLAGLLTAAAALFVGPLSFIGLIAPHLARLAGLGR
PLQQGIGAVLIGAGLMVVSDWLARTVAFPYQLPLGLFAALLAGPYLVWLLGRSNARTP
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