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LOCUS WP_000858484 425 aa linear BCT 28-MAR-2023 ACCESSION WP_000858484 VERSION WP_000858484.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 425) AUTHORS Quistgaard,E.M., Low,C., Guettou,F. and Nordlund,P. TITLE Understanding transport by the major facilitator superfamily (MFS): structures pave the way JOURNAL Nat Rev Mol Cell Biol 17 (2), 123-132 (2016) PUBMED 26758938 REFERENCE 2 (residues 1 to 425) AUTHORS Yan,N. TITLE Structural Biology of the Major Facilitator Superfamily Transporters JOURNAL Annu Rev Biophys 44, 257-283 (2015) PUBMED 26098515 REFERENCE 3 (residues 1 to 425) AUTHORS Yan,N. TITLE Structural advances for the major facilitator superfamily (MFS) transporters JOURNAL Trends Biochem Sci 38 (3), 151-159 (2013) PUBMED 23403214 REFERENCE 4 (residues 1 to 425) AUTHORS Law,C.J., Maloney,P.C. and Wang,D.N. TITLE Ins and outs of major facilitator superfamily antiporters JOURNAL Annu Rev Microbiol 62, 289-305 (2008) PUBMED 18537473 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10017491 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..425 /organism="Enterobacteriaceae" /db_xref="taxon:543" Protein 1..425 /product="nucleoside permease" /GO_function="GO:0015506 - nucleoside:proton symporter activity [Evidence IEA]" /GO_function="GO:0022857 - transmembrane transporter activity [Evidence IEA]" /GO_process="GO:0015858 - nucleoside transport [Evidence IEA]" /GO_process="GO:0055085 - transmembrane transport [Evidence IEA]" /calculated_mol_wt=47228 Region 1..419 /region_name="2A0110" /note="nucleoside transporter; TIGR00889" /db_xref="CDD:129967" Site order(14..15,18..19,22,54,105..106,108..110,113,131, 134..135,138,218,221..222,225..227,230,255,259,313..314, 318,322,338,341..342,345..346,349) /site_type="other" /note="putative chemical substrate binding pocket [chemical binding]" /db_xref="CDD:340866" ORIGIN 1 mkttaklsfm mfvewfiwga wfvplwlwls ksgfsageig wsyactaiaa ilspilvgsi 61 tdrffsaqkv lavlmfagal lmyfaaqqtt fagffpllla ysltymptia ltnsiafanv 121 pdverdfpri rvmgtigwia sglacgflpq ilgyadispt nipllitags sallgvfaff 181 lpdtppkstg kmdikvmlgl dalillrdkn flvfffcsfl famplafyyi fangyltevg 241 mknatgwmtl gqfseiffml alpfftkrfg ikkvlllglv taairygffi ygsadeyfty 301 allflgillh gvsydfyyvt ayiyvdkkap vhmrtaaqgl itlccqgfgs llgyrlggvm 361 mekmfayqep vngltfnwsg mwtfgavmia iiavlfmiff resdneitai kvddrdialt 421 qgevk