Comparing Pf1N1B4_5938 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5938 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P61887 Glucose-1-phosphate thymidylyltransferase 2; G1P-TT 2; dTDP-glucose pyrophosphorylase 2; dTDP-glucose synthase 2; EC 2.7.7.24 from Escherichia coli (strain K12) (see paper)
71% identity, 100% coverage: 1:292/292 of query aligns to 1:292/293 of P61887
4b5bA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 4:289/293 of 4b5bA
4b4gA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 4:289/293 of 4b4gA
4b42A Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 4:289/293 of 4b42A
4b3uA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 10:295/299 of 4b3uA
4asyA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 4:289/293 of 4asyA
4asjA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 3:288/292 of 4asjA
1g3lA The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). Tdp-l-rhamnose complex. (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 3:288/292 of 1g3lA
1g2vA The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). Ttp complex. (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 3:288/292 of 1g2vA
1g1lA The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). Tdp-glucose complex. (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 3:288/292 of 1g1lA
Sites not aligning to the query:
1g0rA The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). Thymidine/glucose- 1-phosphate complex. (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 3:288/292 of 1g0rA
1fxoA The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (rmla). Tmp complex. (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 3:288/292 of 1fxoA
1mc3A Crystal structure of rffh (see paper)
72% identity, 99% coverage: 1:290/292 of query aligns to 2:291/291 of 1mc3A
4b4mA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 7:292/296 of 4b4mA
4b2xB Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 13:298/302 of 4b2xB
4arwA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor (see paper)
73% identity, 98% coverage: 2:287/292 of query aligns to 5:290/294 of 4arwA
5fyeA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor
73% identity, 98% coverage: 2:287/292 of query aligns to 7:292/296 of 5fyeA
5fu8A Pseudomonas aeruginosa rmla in complex with allosteric inhibitor
73% identity, 98% coverage: 2:287/292 of query aligns to 8:293/297 of 5fu8A
5fu0A Pseudomonas aeruginosa rmla in complex with allosteric inhibitor
73% identity, 98% coverage: 2:287/292 of query aligns to 7:292/296 of 5fu0A
5ftvA Pseudomonas aeruginosa rmla in complex with allosteric inhibitor
73% identity, 98% coverage: 2:287/292 of query aligns to 7:292/296 of 5ftvA
>Pf1N1B4_5938 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5938
MKGIILAGGSGTRLHPITRGVSKQLLPVYDKPMIYYPLSVLMLAGIREILIISTPQDLPN
FQNLLGDGSSFGIELSYAEQPSPDGLAQAFLIGEDFIGDSNVALILGDNIFYGYGFSALL
REASQRQTGATVFGYRVSDPDRFGVVEFDDNGKAISIEEKPKHPKSDHAVTGLYFYDNDV
VSIAKQVKPSIRGELEITDVNNAYLQRGDLHVSVLGRGFAWLDTGTHDSLMEAGHFVQTI
EARQGLKVACLEEVAYHQGWLSAAELDKQATALHKTGYGQYLARVLNTEPAK
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory