ID A0A2I0AE63_9ASPA Unreviewed; 776 AA.
AC A0A2I0AE63;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN Name=CYP {ECO:0000313|EMBL:PKA53844.1};
GN ORFNames=AXF42_Ash011324 {ECO:0000313|EMBL:PKA53844.1};
OS Apostasia shenzhenica.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Apostasioideae; Apostasia.
OX NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA53844.1, ECO:0000313|Proteomes:UP000236161};
RN [1] {ECO:0000313|EMBL:PKA53844.1, ECO:0000313|Proteomes:UP000236161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC TISSUE=Stem {ECO:0000313|EMBL:PKA53844.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00007365}.
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DR EMBL; KZ451988; PKA53844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0AE63; -.
DR STRING; 1088818.A0A2I0AE63; -.
DR OrthoDB; 472968at2759; -.
DR Proteomes; UP000236161; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
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 PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PKA53844.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 10..174
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 181..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..308
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 87615 MW; F0E8DA40DC782CA3 CRC64;
MAKTRNPTVF LDVSIDGGRP RRMVFELFSD VVPKTAENFR ALCTGEMGNG PITGKLLHYK
GSIFHRIIKG FMAQGGDFSR RDGTGGESIY GAKYPDENFT LKHDGPGLLS MANAGRDTNG
SQFFITFKAT PHLDGKHVVF GKLIAGHEVL KRIEHVEVDD SKPVVPVKIV DCGEIHDRQN
EETLVRNEKQ KGKLRLSKDV SSSADSEGKR KRKHKKSHKR RKKRKRRHYS SYSDTSSDTD
TELSDTESDS DSSSSLSSST DFSSSSDDRY RKRKKKHSRR DKYKRAKRKR DKKRERRHKR
HKKRSRRKSK WISESDTEEL SSEEDGDNHD RSKKSISHVS VENQNALILE KEATANQLVE
EDITAEPSGE VVKFSKHNGE FLSNGITEEK SIRSHELLPA VAPKEIKSRS QSMSPLHCTS
KSMSPRSHSK SPPAVLSPRM PSRSPSNLSP RDSISRSSGR RSISQSPTRR SISASPIRRN
TSKSPVDKRR SPVELRRRSI TRSRSRSPAR LRERDERGSI SRNSLRSPWK RSTSRSPIKS
SGRRISSRSP ARSSGRSASR SPVRPRPRRT LSRSPIRKSL SRSGSPNGSP RRIRRGRGFS
QRYSYARRYR TPSPDRSPIR FHRYGGRNDR DRYSSYRSYR DRSPPRRYRS PLRYRGRSRS
LSRSPVGYRG RGRGGYSRSP IRSRSPSPER PRYHGSSIPE GTRAAKRRSV SPNRSPSGSR
SRSKSSSSGD TPSPRRASGE KVISRSRSSS PNEKKKGLVS YGEATPDSTG PKGGGV
//
