ID APKA_ARATH STANDARD; PRT; 410 AA. AC Q06548; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE PROTEIN KINASE APK1A (EC 2.7.1.-). GN APK1A. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; eudicotyledons; core eudicots; Rosidae; eurosids II; OC Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=93081726; PubMed=1450380; RA Hirayama T., Oka A.; RT "Novel protein kinase of Arabidopsis thaliana (APK1) that RT phosphorylates tyrosine, serine and threonine."; RL Plant Mol. Biol. 20:653-662(1992). CC -!- FUNCTION: POSSIBLE BI-FUNCTIONAL KINASE. IN VITRO, IT EXHIBITS CC SERINE/THREONINE ACTIVITY. IN VIVO, CAN PHOSPHORYLATE TYROSINE CC RESIDUES OF LIMITED SUBSTRATES. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D12522; BAA02092.1; -. DR HSSP; P11362; 1FGI. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; Tyrosine-protein kinase; KW ATP-binding; Multigene family; Myristate. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT DOMAIN 68 352 PROTEIN KINASE. FT NP_BIND 74 82 ATP (BY SIMILARITY). FT BINDING 106 106 ATP (BY SIMILARITY). FT ACT_SITE 203 203 BY SIMILARITY. SQ SEQUENCE 410 AA; 45519 MW; 5BAB28D9E0065082 CRC64; MGICLSAQVK AESSGASTKY DAKDIGSLGS KASSVSVRPS PRTEGEILQS PNLKSFSFAE LKSATRNFRP DSVLGEGGFG CVFKGWIDEK SLTASRPGTG LVIAVKKLNQ DGWQGHQEWL AEVNYLGQFS HRHLVKLIGY CLEDEHRLLV YEFMPRGSLE NHLFRRGLYF QPLSWKLRLK VALGAAKGLA FLHSSETRVI YRDFKTSNIL LDSEYNAKLS DFGLAKDGPI GDKSHVSTRV MGTHGYAAPE YLATGHLTTK SDVYSFGVVL LELLSGRRAV DKNRPSGERN LVEWAKPYLV NKRKIFRVID NRLQDQYSME EACKVATLSL RCLTTEIKLR PNMSEVVSHL EHIQSLNAAI GGNMDKTDRR MRRRSDSVVS KKVNAGFARQ TAVGSTVVAY PRPSASPLYV //