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Database: UniProt
Entry: A0A0A0LII7_CUCSA
LinkDB: A0A0A0LII7_CUCSA
Original site: A0A0A0LII7_CUCSA 
ID   A0A0A0LII7_CUCSA        Unreviewed;       361 AA.
AC   A0A0A0LII7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=Csa_2G234600 {ECO:0000313|EMBL:KGN61735.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN61735.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN61735.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX   PubMed=19881527; DOI=10.1038/ng.475;
RA   Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA   Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA   Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA   Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA   Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA   Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA   Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA   Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA   Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA   Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA   Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA   Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT   "The genome of the cucumber, Cucumis sativus L.";
RL   Nat. Genet. 41:1275-1281(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00007365}.
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DR   EMBL; CM002923; KGN61735.1; -; Genomic_DNA.
DR   RefSeq; XP_011649200.1; XM_011650898.1.
DR   AlphaFoldDB; A0A0A0LII7; -.
DR   STRING; 3659.A0A0A0LII7; -.
DR   EnsemblPlants; KGN61735; KGN61735; Csa_2G234600.
DR   GeneID; 101207288; -.
DR   Gramene; KGN61735; KGN61735; Csa_2G234600.
DR   KEGG; csv:101207288; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   OMA; QDDGICN; -.
DR   OrthoDB; 339082at2759; -.
DR   Proteomes; UP000029981; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd01926; cyclophilin_ABH_like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          7..172
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REPEAT          298..331
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   361 AA;  40177 MW;  5AF3CC974CA3328C CRC64;
     MPMPRCFLDI TIGGELEGRI IIELYNHLVP KTAENFRALC TGEKGISPNT ALPLHFKGVC
     FHRVIKGFMI QGGDISAGDG TGGESIYGLK FEDENFELKH ERKGMLSMAN SGPNTNGSQF
     FITTTRAPHL DGNHVVFGKV VKGMGVVRSI EHVITGENDR PTLDVVIADC GEIPEGAHDG
     VSNLFKDGDT FPDWPADLDQ SPFELSWWMS AVDSIKAFGN VHFKKQDYKM ALRKYRKALR
     YLDICWEREG IDEEKSTCLR KTKSQIFTNS SACKLKLGDL KGALLDTEFA IREGVNNVKA
     VFRQGQAHMA LNDIDSAVES FKRALDLEPN DAGIKKELAA AKKKIADRRD QERKAYGKMF
     L
//
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