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LOCUS WP_004150785 402 aa linear BCT 20-JUL-2024 ACCESSION WP_004150785 VERSION WP_004150785.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 402) AUTHORS Aravind,L. and Koonin,E.V. TITLE The HD domain defines a new superfamily of metal-dependent phosphohydrolases JOURNAL Trends Biochem Sci 23 (12), 469-472 (1998) PUBMED 9868367 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 13391297 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..402 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..402 /product="HD-GYP domain-containing protein" /EC_number="3.1.4.-" /GO_function="GO:0016787 - hydrolase activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /calculated_mol_wt=45655 Region <5..>107 /region_name="HDGYP" /note="HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms]; COG2206" /db_xref="CDD:441808" Region 103..378 /region_name="HDGYP" /note="HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms]; COG2206" /db_xref="CDD:441808" ORIGIN 1 mrialksalm lttrviqiin pevhrhmqrt alialtlaqr lelpderqqt ifcaallhdi 61 gvlgdkrtih sldaidnihd phqrqgvaml eglatfqpiv pfirdhhfsp nhrgsreqhi 121 vyfadaferl lpadshvaaw ptravveqfv alhreidppl cdilcevaen anfwqhlhpg 181 hiqrlleiig pintryldih glkdvcllia kivdtyssft athsimvgei arqlarwmql 241 peptcqqiqi agylhdigkv yiplsileke gelddeelsq vrehsymtge llsdyselgd 301 iinwasnhhe kmdgsgyplh lekehltlad riisiadift altedrpyrk gmawqealqi 361 meadvingal dsdvflvlrh haetlhaiil qtlaplhser rl