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LOCUS WP_004151767 417 aa linear BCT 28-MAR-2023 ACCESSION WP_004151767 VERSION WP_004151767.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 417) 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 417) 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 417) 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 417) 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..417 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..417 /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=46105 Region 1..414 /region_name="2A0110" /note="nucleoside transporter; TIGR00889" /db_xref="CDD:129967" Site order(14..15,18..19,22,55,106..107,109..111,114,136, 139..140,143,217,220..221,224..226,229,264,268,321..322, 326,330,346,349..350,353..354,357) /site_type="other" /note="putative chemical substrate binding pocket [chemical binding]" /db_xref="CDD:340866" ORIGIN 1 mnlklqlkil sflqfclwgs wlttlgsymf vtlkfdgaai gavysslgia avlmptllgi 61 vadkwisakw vyaichlvga ltlylaaqvt tpgemflvil lnslaymptl glintisyyr 121 lqsagldivt dfppiriwgt igfilamwgv sfsgfelshm qlyigatlsv lltlftltlp 181 hipvanaqrn qswaemlgln afalfknkrm aiffifsmml gaelqitnmf gntflhsfdk 241 dplfagsfiv ehasvlmsis qisetlfilt ipfflsrygi knvmlisiva wmlrfglfaf 301 gdptpfgtvl lvlsmivygc afdffnisgs vfvekevrpe irasaqgmfl mmtngfgcil 361 ggmvsgkvve hftvegitdw qsvwlifagy slvlafafva lfkykhvrqp taaqqsv