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Peptidyl-prolyl cis-trans isomerase, chloroplastic (PPIase) (EC 5.2.1.8) (Cyclophilin) (Cyclosporin A-binding protein) (CYP B) (Rotamase)

 CYPB_VICFA              Reviewed;         248 AA.
Q41651;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 85.
RecName: Full=Peptidyl-prolyl cis-trans isomerase, chloroplastic;
Short=PPIase;
EC=5.2.1.8;
AltName: Full=Cyclophilin;
AltName: Full=Cyclosporin A-binding protein;
Short=CYP B;
AltName: Full=Rotamase;
Flags: Precursor;
Vicia faba (Broad bean) (Faba vulgaris).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Vicia.
NCBI_TaxID=3906;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
CHARACTERIZATION.
TISSUE=Leaf;
PubMed=8061522; DOI=10.1105/tpc.6.6.885;
Luan S., Lane W.S., Schreiber S.L.;
"pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin
from fava bean.";
Plant Cell 6:885-892(1994).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
its effects via an inhibitory action on PPIase.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
-!- TISSUE SPECIFICITY: Highly expressed in leaf.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
{ECO:0000305}.
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EMBL; L32095; AAA64430.1; -; mRNA.
PIR; T12096; T12096.
ProteinModelPortal; Q41651; -.
SMR; Q41651; -.
GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
GO; GO:0006457; P:protein folding; IEA:InterPro.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
1: Evidence at protein level;
Chloroplast; Direct protein sequencing; Isomerase; Plastid; Rotamase;
Transit peptide.
TRANSIT 1 ? Chloroplast. {ECO:0000255}.
CHAIN ? 248 Peptidyl-prolyl cis-trans isomerase,
chloroplastic.
/FTId=PRO_0000025477.
DOMAIN 85 243 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
SEQUENCE 248 AA; 26547 MW; B9688620D40AC257 CRC64;
MASSFSTQLV QSQNLLPRFH AVQGKPHVVS SIGCSKLSST YHYAPRLSVS QQSKAKSITS
RRITCASGAQ GEVAELQAKV TSKIFFDIEI GGESAGRIVI GLFGDAVPKT VENFKTLSTG
AKGYGYQGSF FHRIIPNFMI QGGDFTEGNG TGGVSIYGSK FEDESFDLKH VGPGVLSMAN
AGPNTNGSQF FICTVPTPWL DNRHVVFGHV IEGLDVVKQL ESQETSKLDN SPKKPCKIAK
SGELPLDG


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