ID A0A200PU92_9MAGN Unreviewed; 345 AA.
AC A0A200PU92;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Tetratricopeptide TPR-1 {ECO:0000313|EMBL:OVA01774.1};
GN ORFNames=BVC80_9075g11 {ECO:0000313|EMBL:OVA01774.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA01774.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA01774.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA01774.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(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:OVA01774.1}.
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DR EMBL; MVGT01004037; OVA01774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200PU92; -.
DR STRING; 56857.A0A200PU92; -.
DR InParanoid; A0A200PU92; -.
DR OrthoDB; 339082at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; IPR001440; TPR_1.
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; PF00515; TPR_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT DOMAIN 7..156
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REPEAT 282..315
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 345 AA; 38367 MW; 7A555B90EBDC77D6 CRC64;
MVNPRCFLDI SIGGELEGRI VVELYSDVVP KTAENFRALC TGEKGIGPNT GFMIQGGDIS
ARDGTGGESI YGLKFEDENF ELKHERKGML SMANSGPNTN GSQFFITTTR TSHLDGKHVV
FGKVIKGMGV VRSIEHVYTG DGDSPSLEVV IADCGEIPEG VDDGTSNFFN DGDTYPDWPA
DLEEKPDEIS WWMEAVASVK AFGNEHYKKQ DYKMALRKYR KALRYLDICW EKDDIDEEKS
SSLRKSKSQI FTNSSACKLK LGDLKGALLD TDFAMRDGED NVKALFRQGQ AYMALNDVDA
AVESFKKALE LEPNDGGIKK ELAAAKKRIA DRRDLERKAY SKMFQ
//
