ID O23614_ARATH PRELIMINARY; PRT; 515 AA. AC O23614; DT 01-JAN-1998 (TrEMBLrel. 05, Created) DT 01-JAN-1998 (TrEMBLrel. 05, Last sequence update) DT 01-FEB-2005 (TrEMBLrel. 29, Last annotation update) DE PSII D1 protein processing enzyme (AT4g17740/dl4905c). GN Name=dl4905c; Synonyms=AT4g17740; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RA Bevan M., Stiekema W., Murphy G., Wambutt R., Pohl T., Terryn N., RA Kreis M., Kavanagh T., Entian K.D., Rieger M., James R., RA Puigdomenech P., Hatzopoulos P., Obermaier B., Duesterhoft A., RA Jones J., Palme K., Ansorge W., Delseny M., Bancroft I., Mewes H.W., RA Schueller C., Chalwatzis N.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RA EU Arabidopsis sequencing project; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE. RA EU Arabidopsis sequencing project; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE. RA Cheuk R., Chen H., Kim C.J., Koesema E., Meyers M.C., Banh J., RA Bowser L., Carninci P., Dale J.M., Goldsmith A.D., Hayashizaki Y., RA Ishida J., Jiang P.X., Jones T., Kamiya A., Karlin-Neumann G., RA Kawai J., Lam B., Lee J.M., Lin J., Liu S.X., Miranda M., Narusaka M., RA Nguyen M., Onodera C.S., Palm C.J., Pham P.K., Quach H.L., Sakurai T., RA Satou M., Seki M., Southwick A., Tang C.C., Toriumi M., Yamada K., RA Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE. RA Cheuk R., Chen H., Kim C.J., Koesema E., Meyers M.C., Banh J., RA Bowser L., Carninci P., Dale J.M., Goldsmith A.D., Hayashizaki Y., RA Ishida J., Jiang P.X., Jones T., Kamiya A., Karlin-Neumann G., RA Kawai J., Lam B., Lee J.M., Lin J., Liu S.X., Miranda M., Narusaka M., RA Nguyen M., Onodera C.S., Palm C.J., Pham P.K., Quach H.L., Sakurai T., RA Satou M., Seki M., Southwick A., Tang C.C., Toriumi M., Yamada K., RA Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE. RA Cheuk R., Chen H., Kim C.J., Shinn P., Bowser L., Carninci P., RA Dale J.M., Hayashizaki Y., Hsuan V.W., Ishida J., Jones T., Kamiya A., RA Karlin-Neumann G., Kawai J., Lam B., Lin J., Miranda M., Narusaka M., RA Nguyen M., Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., RA Seki M., Southwick A., Toriumi M., Wong C., Wu H.C., Yamada K., Yu G., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: The enzyme shows specific recognition of a C- CC terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala CC or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, CC but then cleaves at a variable distance from the C-terminus. A CC typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala- CC Leu-Ala-Ala. In the plant chloroplast, the enzyme removes the C- CC terminal extension of the D1 polypeptide of photosystem II. CC -!- SIMILARITY: Contains 1 PDZ/DHR domain. 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; Z97344; CAB10554.1; -. DR EMBL; AL161547; CAB78777.1; -. DR EMBL; AY054171; AAL06832.1; -. DR EMBL; BT006343; AAP21151.1; -. DR EMBL; AF424602; AAL11596.1; -. DR PIR; E71447; E71447. DR HSSP; O04073; 1FC7. DR MEROPS; S41.002; -. DR GO; GO:0005739; C:mitochondrion; IDA. DR InterPro; IPR001478; PDZ. DR InterPro; IPR005151; Peptidase_S41. DR InterPro; IPR004447; Peptidase_S41A. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF03572; Peptidase_S41; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00245; TSPc; 1. DR TIGRFAMs; TIGR00225; prc; 1. DR PROSITE; PS50106; PDZ; 1. KW Hydrolase; Protease; Serine protease. SQ SEQUENCE 515 AA; 55762 MW; 704BE277C41F0F52 CRC64; MEVLASSSLS PISFTKPNKI NPNFSIQVKL WVKQPPKISK ASKFSYARSR SNISRSNAAN PGVVFVCNRF LCVIERNDQR KLSGKVMMKS SVNFRQNLSV ALVRIVSVLL VSSISVVTTD SPPSWGLTEE NLLFLEAWRT IDRAYIDKTF NGQSWFRYRE TALRNEPMNT REETYMAIKK MVATLDDPFT RFLEPGKFKS LRSGTQGAVT GVGLSIGYPT ASDGPPAGLV VISAAPGGPA NRAGILPGDV IQGIDNTTTE TLTIYDAAQM LQGPEGSAVE LAIRSGPETR LLTLTRERVS VNPVKSRLCE LPGSGSNSPK IGYIKLTTFN QNASSAVREA IETLRGNNVN AFVLDLRDNS GGSFPEGIEI AKFWLDKGVI VYICDSRGVR DIYDTDGSNA IATSEPLAVL VNKGTASASE ILAGALKDNK RALVYGEPTY GKGKIQSVFE LSDGSGLAVT VARYETPAHT DIDKVGVTPD HPLPKSFPKD EEAFCGCLKD PTAACYLNQG LLFSR //