SitesBLAST
Comparing Pf1N1B4_1341 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1341 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)
37% identity, 90% coverage: 34:335/336 of query aligns to 26:316/318 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 (= R307) 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)
38% identity, 83% coverage: 58:336/336 of query aligns to 53:331/332 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 (= R307) 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)
40% identity, 99% coverage: 3:336/336 of query aligns to 2:327/330 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)
32% identity, 85% coverage: 53:336/336 of query aligns to 377:658/660 of P06972
- R390 (= R65) Interaction with FhuD; mutation to A: Decreased binding to ferrichrome-FhuD.
- M484 (≠ V161) 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 (≠ A169) 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 (≠ N172) 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 (≠ S184) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-510.
- T510 (≠ F188) mutation to A: Decreased binding to ferrichrome-FhuD; when associated with A-507.
- S515 (≠ G193) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-517.
- Y517 (≠ L201) Interaction with FhuD; mutation to A: Loss of binding to ferrichrome-FhuD; when associated with A-515.
- Q636 (≠ D314) mutation to A: Decreased binding to ferrichrome-FhuD.
Sites not aligning to the query:
- 57 S→A: Decreased binding to ferrichrome-FhuD.
- 170 D→A: Loss of binding to ferrichrome-FhuD; when associated with A-171.
- 171 Q→A: Loss of binding to ferrichrome-FhuD; when associated with A-170.
- 175 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-484; 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-484; L-492 and L-495.
- 182 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-184.
- 184 Interaction with FhuD; T→A: Loss of binding to ferrichrome-FhuD; when associated with A-182.
- 304 Interaction with FhuD; E→A: Decreased binding to ferrichrome-FhuD.
Query Sequence
>Pf1N1B4_1341 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1341
MIDRRYALLLTVLGALLLVSCVVSLGAGPARVPVDVVWRILLHKILGFGVPDWTAGQEHI
VWLIRVPRMLLGALVGAGLALIGAVLQAVTRNPLADPHLLGVTSGATLGAVIVVLHVGEI
VGLLTLPIAAFIGALLSMLIVLMIANRHGRLDSDRLLLCGVAVSFVMMAIANLLLFLGDH
RASSAVMFWMLGGLGLARWELLAVPAASVLLGLVLLLGMARPLNALMAGEQTAVTLGLNA
RTVRLRVFLIASLMTGVLVSISGSIGFVGLMVPHIARRLVGAEHRRLLPVCVLLGSLFLV
WVDVAARTLIAPEDLPIGVATAAIGGLFFIGLMRRR
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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