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Figure 1 | BMC Plant Biology

Figure 1

From: Identification and characterization of plant Haspin kinase as a histone H3 threonine kinase

Figure 1

Multiple alignment of Haspin kinases in the kinase domain. (A) Kinase domains from Anopheles gambiae (EAA05110), Aquilegia caerulea (AcoGoldSmith_v1.025146m), Arabidopsis rylata (XP_002889750), Arabidopsis thaliana (NP_172416), Aspergillus fumigatus (XP_751829), Aspergillus nidulans (XP_659658), Brachypodium distachyon (Bradi1g20070.1), Caenorhabditis elegans F22H10.5 (NP_510696), C. elegans C01H8.9 (NP_492043), C. elegans Y18H1A.10 (NP_490768), Carica papaya (evm.model.supercontig_48.218), Chlamydomonas reinhardtii (XP_001699957), Chlorella variabilis (EFN57276), Cucumis sativus (Cucsa.050880.1), Drosophila melanogaster (P83103), Encephalitozoon cuniculi (NP_597598), Gallus gallus (XP_425408), Glycine max 03g38780 (Glyma03g38780.1), G. max 19g41380 (Glyma19g41380.1), Homo sapiens (AAH47457), Manihot esculenta (cassava4.1_028012m), Medicago truncatula (AC235094_20.1), M. truncatula (Medtr7g135040.1), Mimulus guttatus (mgv1a027116m), Micromonas pusilla (XP_003057374), Micromonas RCC299 (XP_002502153), Mus musculus (NP_034483), Physcomitrella patens (XP_001777245), Populus trichocarpa (XP_002329997), Prunus persica (ppa015455m), Oryza sativa (BAC16406), Ostreococcus lucimarinus (XP_001417826), Ostreococcus tauri (XP_003079484), Ricinus communis (XP_002512572), Saccharomyces cerevisiae Ybl009wp (NP_009544), S. cerevisiae ALK-1 (CAA61012), Schizosaccharomyces pombe (CAB16874), Selaginella moellendorffii (XP_002986955), Setaria italica (SiPROV006697m), Tetraodon nigroviridis (CAF92724), Vitis vinfera (XP_002276683), Volvox carteri (XP_002952488), Xenopus laevis (TC388096), and Zea mays (NP_001149827). Accession numbers from the DNA Data Bank of Japan (DDBJ) or transcript names from the genome database (Phytozome v6.0) are given in parentheses. (B) Amino acid structure of Haspin proteins from A. thaliana, H. sapiens, and S. pombe. Black boxes show NLSs (nuclear localization signals) predicted by the PSORT algorithm (http://psort.nibb.ac.jp/form.html). Gray box indicates kinase domain. (C) Multiple alignment of kinase domain of AtHaspin, human Haspin, and fission yeast Haspin. Missing residues are shown as dashes, identical amino acids are shaded in gray, and residues of ATP/Mg2+ ion-binding sites are shown in magenta. Important residues for histone H3 phosphorylation in catalytic cleft are shown in green.

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