SitesBLAST
Comparing CCNA_03372 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 1 hits to proteins with known functional sites (download)
Q9HY80 Bacterioferritin-associated ferredoxin; Bfd from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
34% identity, 97% coverage: 1:59/61 of query aligns to 1:59/73 of Q9HY80
- Y2 (= Y2) mutation to A: Does not bind [2Fe-2S] cluster.; mutation to F: Wild-type iron release from BfrB, 3-fold decreased affinity for BfrB.
- C4 (= C4) binding [2Fe-2S] cluster
- L5 (≠ N5) mutation to A: 2-fold decreased iron release from BfrB, 25-fold decreased affinity for BfrB.
- C6 (= C6) binding [2Fe-2S] cluster
- R26 (≠ A26) binding phosphate; mutation to E: No significant change in structure, [2Fe-2S] cluster or iron mobilization from BfrB, in truncated protein. No significant change in structure, [2Fe-2S] cluster or iron mobilization from BfrB, in truncated protein; when associated with Y-46.
- R29 (≠ F29) binding phosphate; mutation to E: Probably unstable, it cannot be overexpressed, in truncated protein.
- C38 (= C38) binding [2Fe-2S] cluster
- K40 (= K40) mutation to A: Wild-type iron release from BfrB, 2-fold decreased affinity for BfrB.
- C41 (= C41) binding [2Fe-2S] cluster
- C43 (= C43) mutation to S: Increases yield of protein and stability of [2Fe-2S] center, no effect on its function.
- K46 (≠ R46) binding phosphate; mutation to E: Probably unstable, it cannot be overexpressed, in truncated protein.; mutation to Y: No significant change in structure, [2Fe-2S] cluster or iron mobilization from BfrB, in truncated protein; when associated with E-26.
Sites not aligning to the query:
- 57:73 mutation Missing: No change in ability to mobilize iron from BfrB.
Query Sequence
>CCNA_03372
MYVCNCNGIREREVRAAIDAGATRPADIFRHKGCQAQCAKCVCEMRQMIQESREALAYAA
E
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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