ID SWE1_YEAST STANDARD; PRT; 819 AA. AC P32944; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE MITOSIS INHIBITOR PROTEIN KINASE SWE1 (EC 2.7.1.-). GN SWE1 OR YJL187C OR J0406. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Hemiascomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94074541. RA BOOHER R.N., DESHAIES R.J., KIRSCHNER M.W.; RT "Properties of Saccharomyces cerevisiae wee1 and its differential RT regulation of p34CDC28 in response to G1 and G2 cyclins."; RL EMBO J. 12:3417-3426(1993). RN [2] RP SEQUENCE FROM N.A. RA OBERMAIER B., PIRAVANDI E., RINKE M., DOMDEY H.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PROTEIN KINASE THAT ACTS BOTH ON SERINES AND ON CC TYROSINES. IT ACTS AS A NEGATIVE REGULATOR OF ENTRY INTO MITOSIS CC (G2 TO M TRANSITION). PHOSPHORYLATES AND INHIBITS CDC28. CC -!- SIMILARITY: WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR- CC PROTEIN KINASES. HIGHLY SIMILAR TO S.POMBE WEE1. 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 -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X73966; CAA52150.1; -. DR EMBL; Z49462; CAA89482.1; -. DR PIR; S39999; S39999. DR PIR; S40400; S40400. DR SGD; L0002248; SWE1. 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 Mitosis; Transferase; Tyrosine-protein kinase; ATP-binding. FT DOMAIN 444 794 PROTEIN KINASE. FT NP_BIND 450 458 ATP (BY SIMILARITY). FT BINDING 473 473 ATP (BY SIMILARITY). FT ACT_SITE 579 579 BY SIMILARITY. SQ SEQUENCE 819 AA; 92467 MW; 8E80154D CRC32; MSSLDEDEED FEMLDTENLQ FMGKKMFGKQ AGEDESDDFA IGGSTPTNKL KFYPYSNNKL TRSTGTLNLS LSNTALSEAN SKFLGKIEEE EEEEEEGKDE ESVDSRIKRW SPFHENESVT TPITKRSAEK TNSPISLKQW NQRWFPKNDA RTENTSSSSS YSVAKPNQSA FTSSGLVSKM SMDTSLYPAK LRIPETPVKK SPLVEGRDHK HVHLSSSKNA SSSLSVSPLN FVEDNNLQED LLFSDSPSSK ALPSIHVPTI DSSPLSEAKY HAHDRHNNQT NILSPTNSLV TNSSPQTLHS NKFKKIKRAR NSVILKNREL TNSLQQFKDD LYGTDENFPP PIIISSHHST RKNPQPYQFR GRYDNDTDEE ISTPTRRKSI IGATSQTHRE SRPLSLSSAI VTNTTSAETH SISSTDSSPL NSKRRLISSN KLSANPDSHL FEKFTNVHSI GKGQFSTVYQ VTFAQTNKKY AIKAIKPNKY NSLKRILLEI KILNEVTNQI TMDQEGKEYI IDYISSWKFQ NSYYIMTELC ENGNLDGFLQ EQVIAKKKRL EDWRIWKIIV ELSLALRFIH DSCHIVHLDL KPANVMITFE GNLKLGDFGM ATHLPLEDKS FENEGDREYI APEIISDCTY DYKADIFSLG LMIVEIAANV VLPDNGNAWH KLRSGDLSDA GRLSSTDIHS ESLFSDITKV DTNDLFDFER DNISGNSNNA GTSTVHNNSN INNPNMNNGN DNNNVNTAAT KNRLILHKSS KIPAWVPKFL IDGESLERIV RWMIEPNYER RPTANQILQT EECLYVEMTR NAGAIIQEDD FGPKPKFFI //