ID O22906 PRELIMINARY; PRT; 230 AA. AC O22906; DT 01-JAN-1998 (TrEMBLrel. 05, Created) DT 01-JAN-1998 (TrEMBLrel. 05, Last sequence update) DT 05-JUL-2004 (TrEMBLrel. 27, Last annotation update) DE Putative peptidyl-prolyl cis-trans isomerase (Single domain DE cyclophilin type peptidyl-prolyl cis-trans isomerase). GN Name=At2g47320; Synonyms=CYP21-3; 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 SEQUENCE FROM N.A. RA Rounsley S.D., Lin X., Ketchum K.A., Crosby M.L., Brandon R.C., RA Spriggs T.A., Mason T.M., Kerlavage A.R., Adams M.D., Somerville C.R., RA Venter J.C.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Town C.D., Kaul S.; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX PubMed=15051864; RA Romano P.G., Horton P., Gray J.E.; RT "The Arabidopsis cyclophilin gene family."; RL Plant Physiol. 134:1268-1282(2004). RN [4] RP SEQUENCE FROM N.A. RA Romano P.G.N., Horton P., Gray J.E.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIases accelerate the folding of proteins. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. 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; AC002337; AAB63832.1; -. DR EMBL; AY568520; AAS75303.1; -. DR PIR; G84913; G84913. DR HSSP; Q27450; 1C5F. DR GO; GO:0016853; F:isomerase activity; IEA. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA. DR GO; GO:0006457; P:protein folding; IEA. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Isomerase; Rotamase. SQ SEQUENCE 230 AA; 26042 MW; 6198D43EE5B9552F CRC64; MAKIKPQALL QQSKKKKGPS RISITNIVIY TLAVLLLVFV LFSAYRRWTH RSEIPTHNGR SVLEDAAFPG MKNVDLPRFA TLDTGKGSVT IELFKDTAPN VVDQFMKFCQ DGYFKGFLFS RVVKHFVIQA GDSAEFDAVK DWALDRKNID TSLKHEEFMV GTPKAKNEQG GFEFFIVSAQ IKDLNEKLTV FGRVSKGQDV VQEIEEVETD DQYQPKSPIE IMSVTLLQDM //