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LOCUS WP_017023794 333 aa linear BCT 01-JAN-2025 ACCESSION WP_017023794 VERSION WP_017023794.1 KEYWORDS RefSeq. SOURCE Vibrio rumoiensis ORGANISM Vibrio rumoiensis Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio. REFERENCE 1 (residues 1 to 333) AUTHORS Wilkens,S. TITLE Structure and mechanism of ABC transporters JOURNAL F1000Prime Rep 7, 14 (2015) PUBMED 25750732 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 333) AUTHORS ter Beek,J., Guskov,A. and Slotboom,D.J. TITLE Structural diversity of ABC transporters JOURNAL J Gen Physiol 143 (4), 419-435 (2014) PUBMED 24638992 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 11418519 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..333 /organism="Vibrio rumoiensis" /db_xref="taxon:76258" Protein 1..333 /product="ABC transporter ATP-binding protein" /GO_function="GO:0016887 - ATP hydrolysis activity [Evidence IEA]" /GO_function="GO:0042626 - ATPase-coupled transmembrane transporter activity [Evidence IEA]" /GO_function="GO:0140359 - ABC-type transporter activity [Evidence IEA]" /calculated_mol_wt=37377 Region 11..333 /region_name="DppD" /note="ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism]; COG0444" /db_xref="CDD:440213" ORIGIN 1 msssdkygkl lvegknlikd fpissstlkq pmmraindvs fkmyksrgla vvgesgsgks 61 ttakmiakmy sptagtieyk grdiqeikkk qdlmhyregv qmvwqdpfgs lnpthnifhh 121 iarpliihnk vkasdkkelq eriyelleqv glnpaketaa kfphqlsggq rqrvnlarni 181 avgaevvlad eptsmldvsi ragvlnlmee mkfdkqmsll yithdiatar yiaedlsvmy 241 vghmvewgdt deiihdpqhp ytqllvsavp dpkksihekl kgnkgeiplw tpesvgcpfa 301 grclhvtdkc rekmpgvtql adnhfvrcyl fek