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LOCUS WP_014342966 443 aa linear BCT 24-DEC-2024 ACCESSION WP_014342966 VERSION WP_014342966.1 KEYWORDS RefSeq. SOURCE Klebsiella pneumoniae ORGANISM Klebsiella pneumoniae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella; Klebsiella pneumoniae complex. REFERENCE 1 (residues 1 to 443) AUTHORS Akritidou,K. and Thurtle-Schmidt,B.H. TITLE OLD family nuclease function across diverse anti-phage defense systems JOURNAL Front Microbiol 14, 1268820 (2023) PUBMED 37840731 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 443) AUTHORS Schiltz,C.J., Adams,M.C. and Chappie,J.S. TITLE The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases JOURNAL Nucleic Acids Res 48 (5), 2762-2776 (2020) PUBMED 32009148 REFERENCE 3 (residues 1 to 443) AUTHORS Schiltz,C.J., Lee,A., Partlow,E.A., Hosford,C.J. and Chappie,J.S. TITLE Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage JOURNAL Nucleic Acids Res 47 (17), 9448-9463 (2019) PUBMED 31400118 REFERENCE 4 (residues 1 to 443) AUTHORS Snider,J., Thibault,G. and Houry,W.A. TITLE The AAA+ superfamily of functionally diverse proteins JOURNAL Genome Biol 9 (4), 216 (2008) PUBMED 18466635 REMARK Publication Status: Online-Only 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 11466458 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..443 /organism="Klebsiella pneumoniae" /db_xref="taxon:573" Protein 1..443 /product="ATP-dependent nuclease" /EC_number="3.1.-.-" /GO_function="GO:0004519 - endonuclease activity [Evidence IEA]" /GO_function="GO:0004527 - exonuclease activity [Evidence IEA]" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_function="GO:0016887 - ATP hydrolysis activity [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /calculated_mol_wt=50846 Region <2..266 /region_name="DUF2813" /note="Protein of unknown function (DUF2813); pfam11398" /db_xref="CDD:431868" Region 267..363 /region_name="TOPRIM_OLD" /note="topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in bacterial and archaeal nucleases of the OLD (overcome lysogenization defect) family. The bacteriophage P2 OLD protein, which has DNase as well as RNase activity; cd01026" /db_xref="CDD:173776" Site order(276..277,280,329,331) /site_type="active" /note="putative active site [active]" /db_xref="CDD:173776" Site order(276,329) /site_type="other" /note="putative metal-binding site [ion binding]" /db_xref="CDD:173776" ORIGIN 1 mfyrlegela eddsvmtlrs fidgegealv leeidelarh lvrlmpvlrl rdarfmrrih 61 ngtvphspqi eitarqldfl srelvshpqn lsdgqirqgl samvqllehy faeqssaqtr 121 hrlmrrrshd eqrswryldi inrmidkpgg rshrvillgl fatllqakgt vrldrdarpl 181 lliedpetrl hpimlsvawh llnllplqrv tttnsgells ltpveqvcrl vrestrvsaw 241 rlgpggmnae esrriafhir fnrasslfar cwllvegete twvinelarq cghhfdaegv 301 kviefaqsgl kplikfarrm giqwhvlvdg deagkkyaat vrgllnndre lerdhltslp 361 aldmehfmyr qgfddvyhrv aqipdnvpmn mrrvitkaih rsskpdlaie vameagrrgv 421 davptllkkm fsrvlwlarg rad