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LOCUS WP_002921896 464 aa linear BCT 31-DEC-2024 [Klebsiella]. ACCESSION WP_002921896 VERSION WP_002921896.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 464) AUTHORS Kane,E.I. and Spratt,D.E. TITLE Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation JOURNAL Int J Mol Sci 22 (2), 609 (2021) PUBMED 33435370 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 464) AUTHORS Li,J., Mahajan,A. and Tsai,M.D. TITLE Ankyrin repeat: a unique motif mediating protein-protein interactions JOURNAL Biochemistry 45 (51), 15168-15178 (2006) PUBMED 17176038 REFERENCE 3 (residues 1 to 464) AUTHORS Mosavi,L.K., Cammett,T.J., Desrosiers,D.C. and Peng,Z.Y. TITLE The ankyrin repeat as molecular architecture for protein recognition JOURNAL Protein Sci 13 (6), 1435-1448 (2004) PUBMED 15152081 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 12356329 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..464 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..464 /product="ankyrin repeat domain-containing protein" /GO_function="GO:0005515 - protein binding [Evidence IEA]" /calculated_mol_wt=48470 Region 27..119 /region_name="Ank_2" /note="Ankyrin repeats (3 copies); pfam12796" /db_xref="CDD:463710" Site order(29,32..34,36..37,41,44,53,55,57,61..62,65..67, 69..70,74,77,86,88,90,94..95,98..100,103..104,108,111) /site_type="other" /note="oligomer interface [polypeptide binding]" /db_xref="CDD:293786" Region 55..86 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" Region 88..117 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" Region 166..414 /region_name="ANKYR" /note="Ankyrin repeat [Signal transduction mechanisms]; COG0666" /db_xref="CDD:440430" Region 185..215 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" Region 217..249 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" Site order(251,253,257..258,261..263,265..266,270,273,282,284, 286,290..291,294..296,298..299,303,306,315,317,319, 323..324,327..329,331..332,336,339,348) /site_type="other" /note="oligomer interface [polypeptide binding]" /db_xref="CDD:293786" Region 251..282 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" Region 284..315 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" Region 317..348 /region_name="ANK repeat" /note="ANK repeat [structural motif]" /db_xref="CDD:293786" ORIGIN 1 mkvikglvll clmmlagcqs eeetsqflla ckydapatia amldngidvd gqdktglsgl 61 mvaaaenrrd vvelllkrra kpnlqtrqgv talmlaaarg sdtaiigdll qagasvnqts 121 idkstalmsa isdggdirnd yqhilamkkp dapveeestl dkivgataak slatgnralm 181 tedmalqlap gafkknvdei valllkhgad vkavnasges afflavdhar saetittlan 241 agadtsladk sgttplmlaa agddpdlvla lsasgvevdq pnregltalq vaagqgapav 301 iaalaqrgak vdqlsandls plmlavkmnn kanveallaa gasvnlsnka gytaigysra 361 gevrqlllaq haelkgqaah maqselqfca nafadklays diaravnndt rpdimrhqqs 421 cpelgeltml lgeftftpag atylgepvtc kvseyrktfe vncr