SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS08855 FitnessBrowser__Pedo557:CA265_RS08855 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 1 hits to proteins with known functional sites (download)

P0AFF4 Nucleoside permease NupG; Nucleoside-transport system protein NupG from Escherichia coli (strain K12) (see paper)
45% identity, 100% coverage: 1:458/459 of query aligns to 1:418/418 of P0AFF4

query
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P0AFF4

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R136 (= R136) mutation to A: Abolishes the binding affinity for uridine.
T140 (= T140) mutation to A: Abolishes the binding affinity for uridine.
F143 (= F143) mutation to A: Abolishes the binding affinity for uridine.
Q225 (= Q226) mutation to A: No change in the binding affinity for uridine.
N228 (= N229) mutation to A: Abolishes the binding affinity for uridine.
Q261 (= Q262) mutation to A: Abolishes the binding affinity for uridine.
E264 (= E265) mutation to A: Abolishes the binding affinity for uridine.
Y318 (= Y318) mutation to A: Abolishes the binding affinity for uridine.
F322 (= F322) mutation to A: Abolishes the binding affinity for uridine.
D323 (= D323) mutation to A: 20-fold increase in the binding affinity for uridine.

Query Sequence

>CA265_RS08855 FitnessBrowser__Pedo557:CA265_RS08855
MNVKFRLTIMSFMQFFVWAAWLITIANYWFGTKQWDGADFGIIFSTMGIASLFMPTITGI
LADKWINAERLYAILHILYAATMFYLPQVEDPHTFFWVILVAMCFYMPTIALSNSISYTT
LKNGNFDVVKNFPPIRVWGTVGFIAAMWLTNLTGNKASANQFYIAGVSALMLGLYSFTLP
ACKPLNLISEKKTFAQKLGLESFKLFADYKMALFFIFSMFLGAALQLTNAYGDVFLDEFK
LFPVFAESFVIRYSTIILSISQISETLFILAIPFFLKRFGIKWVIAIAMFAWVLRFGLFA
FGDPSTNLWMIITSCIVYGMAFDFFNISGSLFVETSTTPKTRSSAQGLFMMMTNGFGAVF
GSLVSGWMINKYFTTYYSSIDSLSKYVKSEADNKHLLQFLKNKGISVLENGNLSRALDVK
DWHNIWLSFTIYVLVIAIVFVVIFKHKHTRAEVEAINHL

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