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Database: UniProt
Entry: A0AAD7QB05_QUISA
LinkDB: A0AAD7QB05_QUISA
Original site: A0AAD7QB05_QUISA 
ID   A0AAD7QB05_QUISA        Unreviewed;       418 AA.
AC   A0AAD7QB05;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   SubName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000313|EMBL:KAJ7978195.1};
GN   ORFNames=O6P43_007698 {ECO:0000313|EMBL:KAJ7978195.1};
OS   Quillaja saponaria (Soap bark tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Quillajaceae; Quillaja.
OX   NCBI_TaxID=32244 {ECO:0000313|EMBL:KAJ7978195.1, ECO:0000313|Proteomes:UP001163823};
RN   [1] {ECO:0000313|EMBL:KAJ7978195.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S10 {ECO:0000313|EMBL:KAJ7978195.1};
RX   PubMed=36952412;
RA   Reed J., Orme A., El-Demerdash A., Owen C., Martin L.B.B., Misra R.C.,
RA   Kikuchi S., Rejzek M., Martin A.C., Harkess A., Leebens-Mack J.,
RA   Louveau T., Stephenson M.J., Osbourn A.;
RT   "Elucidation of the pathway for biosynthesis of saponin adjuvants from the
RT   soapbark tree.";
RL   Science 379:1252-1264(2023).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00007365}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAJ7978195.1}.
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DR   EMBL; JARAOO010000003; KAJ7978195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD7QB05; -.
DR   KEGG; qsa:O6P43_007698; -.
DR   Proteomes; UP001163823; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016018; F:cyclosporin A binding; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:TreeGrafter.
DR   CDD; cd10017; B3_DNA; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 1.
DR   InterPro; IPR003340; B3_DNA-bd.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D-RELATED; 1.
DR   Pfam; PF00160; Pro_isomerase; 2.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM01019; B3; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF101936; DNA-binding pseudobarrel domain; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000313|EMBL:KAJ7978195.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP001163823};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          7..138
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   418 AA;  46314 MW;  32468E0D28162B3A CRC64;
     MSNPKVFFDI LIGKTKAGRV VMELFADATP KTAENFRALC TGGKGIGRSG KLLHYKGSTF
     HRIIPNFMWP GILSMANAGP NTNGSQFFIC TEKTPWLDGK HVVFGKIVDG YSVVKEMEKV
     GSDSGSTSEK VVIEDCDPLN SSLSLFSLSG DPVTTGVEKK QSTMAENSKG KQWKGKGVVS
     YDSDEETGAA LALASLKHQK LDEKTTKELH QLKIKFLGKD RANPDPLVVK SKSKGLKIHG
     SAKGSAMKSK IGSNSPIKNS RGQQRLTLFS DKHALPRFPL LPNYLQFIIG NCSQPFEKQL
     TETDVNGAQS RLALNKSDVE ECILPLLNNK ENLIVGVPVT TFDLDGREFP MVFKYWPNKI
     YVLNGGWKAF SEAYKLRKNE DFVTVWMFRN AITRNLCFVI GVRRLPVFQP LKKRGSNK
//
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