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Database: UniProt
Entry: A0A2J6JUQ2_LACSA
LinkDB: A0A2J6JUQ2_LACSA
Original site: A0A2J6JUQ2_LACSA 
ID   A0A2J6JUQ2_LACSA        Unreviewed;       361 AA.
AC   A0A2J6JUQ2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=PPIase cyclophilin-type domain-containing protein {ECO:0000259|PROSITE:PS50072};
GN   ORFNames=LSAT_4X168960 {ECO:0000313|EMBL:PLY66551.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY66551.1};
RN   [1] {ECO:0000313|EMBL:PLY66551.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PLY66551.1}.
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DR   EMBL; NBSK01009858; PLY66551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6JUQ2; -.
DR   STRING; 4236.A0A2J6JUQ2; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_4X168960_mrna; cds-PLY66551.1; gene-LSAT_4X168960.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_4X168960_mrna; cds-PLY66551.1; gene-LSAT_4X168960.
DR   OrthoDB; 339082at2759; -.
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; 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; 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   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;  40350 MW;  DD35917074BA1E8E CRC64;
     MANPRCYLDI SIGGELEGRL VVELYKDIVP KTAENFRALC TGEKGIGPNT GVPLHLKGSC
     FHRVIKGFMI QGGDISARNG TGGESIYGLK FEDENFELKH ERKGMLSMAN SGPNTNGSQF
     FITTTRTSHL DGKHVVFGRV IKGMGVVRSV EHTTTVENDL PIQEVVIQDC GELLEGEDDG
     VCDFFKDGDT YPDWPLDLDV KPEEVSWWMT AVDAIKAFGN EQFKKQDYKN ALRKYRKALR
     YLDICWEKED IDEGKTDSLR KTKSQIFTNS SACKLKLGDL KGALLDADFA LREMDDNVKA
     LFRQGQASMA LNDIDSAVES FKKALVLEPN DGGIKKELAA AKKRIADRRD QEKKAFARMF
     K
//
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